Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

9700 > biomolecules > Flashcards

biomolecules Flashcards

1
Q

biomolecules

A

they are molecules involved in the maintenance and metabolic reactions in a living organism

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

elements of carbohydrates

A

C,H,O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

elements of proteins

A

C,H,O,N,S

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

examples of proteins

A

methionine,cysteine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

elements of lipids

A

C,H,O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Elements of nucleic acids

A

C,H,O,N.P

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

are carbohydrates a polymer or macromolecule

A

they are both polymers and macromolecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

are proteins polymers or macromolecules

A

macromolecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

are lipids polymers or macromolecules

A

macromolecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

are nucleic acids polymers or macromolecules

A

macromolecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

carbohydrates building blocks

A

monosaccharide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

proteins building blocks

A

amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

lipids building blocks

A

fatty acids and glycerol

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

nucleic acid building blocks

A

nucleotide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

carbohydrate:

A
  • hydrates of carbon
  • ratio of H to O is 2:1( if its not 2:1 its a lipid)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

the general formula of carbohydrates are

A

Cn(H2O)n

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

classification of biomolecules can be made based on

A

1)behavior during hydrolysis
2)based on functional groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

what happens during hydrolysis

A

water is added, bond is broken

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

monosaccharide:

A

carbohydrates that cannot be hydrolysed further into a simpler unit ( example: glucose)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

disaccharide:

A

gives 2 monosaccharide units on hydrolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

examples of disaccharide hydrolysis reactions

A

maltose-> glucose + glucose
lactose-> glucose + galactose
sucrose-> glucose + fructose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

polysaccharide

A

gives many monosaccharides unit on hydrolysis (example: starch and glycogen- functional) (example: cellulose- structural)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

ketose- ketone ( functional group)

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

aldose- aldehyde( functional group)

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

triose (3 carbon atoms)

A

C3H6O3
- monosaccharide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

tetrose( 4 carbon atoms)

A

C4H8O4
- monosaccharide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Pentose( 5 carbon atoms)

A

C5H10O5
- monosaccharide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Pentose sugar examples:

A
  • ribose sugar (RNA)
  • deoxyribose sugar (DNA)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

hexose (6 carbon atoms)

A

C6H12O6
- monosaccharide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Hexose sugar examples

A
  • glucose
  • fructose
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

glucose formula

A

C6H12O6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

glucose short

A

hexose, monosaccharide, aldose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

role of glucose

A

release energy by breaking down of bonds, building blocks of polysaccharides like starch, cellulose and glycogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q
A

glucose straight chain formula

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q
A

alpha glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q
A

beta glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

Ring structures of alpha and beta glucose

A
  • ring structures are stable
    -first carbon atoms double bond break and the 5th carbon atom sacrifices its OH group to the first carbon atom.
  • ring is formed between 1st and 5th carbon atom
  • alpha and beta glucose are isomers
  • glucose has pyranose ring
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

pyranose

A

six corner ring

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

similarities between alpha and beta glucose

A

pyranose ring, same number of carbon , hydrogen and oxygen, both are isomers, same number of bonds.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

beta glucose

A

-OH group of first atom is above the plane of the ring
- cellulose is made up of beta glucose and is more stable
- solidly packed molecules, cannot be broken down

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

alpha glucose

A
  • OH group of the first carbon is below the plane of the ring
  • starch and glycogen is made up of alpha glucose and is not very stable
    -molecules are compressed but can be easily taken apart
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

fructose short

A

ketose, hexose, furanose ring

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

furanose

A

5 corner ring

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q
A

fructose straight chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q
A

alpha fructose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q
A

beta fructose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

similarities between glucose and fructose

A

isomers, same number of Carbon, hydrogen and oxygen. same number of bonds, monosaccharides.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

glucose long

A

pyranose ring, ring formed between between 1st and 5th carbon atom, aldose , energy source

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

fructose long

A

furanose ring, ring formed between 2nd and 5th carbon atom. not and energy source

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

properties of monosaccharides

A
  • sweet in taste
  • soluble in water
  • reducing sugar (+ test with benedicts solution)
  • building blocks of polysaccharides
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

disaccharides long

A

made up of 2 monosaccharides formed by the condensation reaction, 1 molecule of water released, glycosidic bond formed.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q
A

alpha glucose+ alpha glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q
A

maltose+ H2O - glycosidic bond formed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

annotation of maltose

A
  • condensation reaction
  • 2 alpha glucose involved
  • water removed, 1,4 glycosidic bond formed
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

alpha glucose + alpha glucose

A

maltose + H2O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

alpha glucose + beta fructose

A

sucrose + H2O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q
A

sucrose formation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

annotation of sucrose

A
  • condensation reaction
  • alpha glucose and beta fructose involved
  • water is removed
  • alpha -1 glucose and beta-2 fructose glycosidic bond
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

properties of disaccharides

A
  • sweet in taste
  • soluble in water when hydrolysed gives 2 monosaccharide units
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

condensation reaction definition

A

a reaction in which 2 molecules are linked together with the release of a water molecule, a new bond is formed (covalent),

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

hydrolysis reaction definition

A

a reaction in which water is added to provide H+ and OH- ions which break down the bond and split large molecules into small ones.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
Q

test for reducing sugar

A

take 2cm^3 of sample, add 2cm^3 of benedicts solution, heat at 90℃, observe the color change. ( blue-> green,yellow,orange, brick red)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
63
Q

reducing sugar

A

acts as a reducing agent, it reduces CuSO4 (Cu2+ into CuO(Cu2+))

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
64
Q

test for non reducing sugar

A

take 2cm^3 of sample, to it add 2cm^3 of dilute HCl. ( to break glycosidic bond) heat it at 90℃. add excess sodium hydrogen carbonate. add 2cm^3 of benedicts solution, heat it at 90℃, observe the color change to brick red

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
65
Q

why add excess sodium hydrogen carbonate?

A

to neutralize benedicts soliton

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
66
Q

polysaccharide example

A

starch

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
67
Q

general formula starch

A

(C6H10O5)n

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
68
Q

starch

A

stored as grains, made up of 2 components: amylose - alpha glucose, unbranched, long straight chain made up of many alpha glucose, joined by alpha 1,4 glycosidic bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
69
Q

amylose chain

A

spiral/helix/curved and coiled up structure. it results in starch to compact and occupy less space/ tightly packed. each turn contains 6 glucose molecules. helix is joined by hydrogen bond which provides stability and helix structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
70
Q
A

amylose chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
71
Q

amylose gives +ve test with iodine

A

which is trapped in helix and forms a poly iodide complex which turns the color of iodine from brown -> blue black. when heated at high temperature, hydrogen bond breaks, helix structure lost, iodine not trapped, color of solution remains brown

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
72
Q

amylopectin

A

80% of starch, branches every 24-30 glucose molecule, bonds alpha 1,4 glycosidic bond and alpha 1,6 glycosidic bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
73
Q
A

amylopectin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
74
Q

bonds in amylopectin

A

alpha 1,6
alpha 1,4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
75
Q

bond in amylose

A

alpha 1,4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
76
Q

branches in amylose

A

unbranched

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
77
Q

amylopectin branches

A

branched

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
78
Q

amylose size

A

small

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
79
Q

amylopectin size

A

large

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
80
Q

amylose shape

A

helical

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
81
Q

amylopectin shape

A

not helical

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
82
Q

amylose with iodine test

A

+ve

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
83
Q

amylopectin with iodine test

A

-ve

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
84
Q

compactness of amylose

A

less compact

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
85
Q

compactness of amylopectin

A

more compact

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
86
Q

cross link amylose

A

No

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
87
Q

cross link in amylopectin

A

Yes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
88
Q

% in amylose

A

20

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
89
Q

% in amylopectin

A

80

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
90
Q

how is the structure of starch adapted for its function

A

many C-C and C-H bonds, breaking up of these bonds releases stored energy . insoluble, does not affect the osmotic balance inside of the cell, bulky in nature, cannot diffuse out, compact, occupies less space, stored as grains.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
91
Q

how is the structure of glycogen adapted for its function

A

many C-C and C-H bonds, breaking up of these bonds releases stored energy . insoluble, does not affect the osmotic balance inside of the cell, bulky in nature, cannot diffuse out, compact, occupies less space, stored as granules.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
92
Q
A

glycogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
93
Q

glycogen

A

alpha glucose, bond 1,4 and alpha glucose 1,6 glycosidic bond branches every 8-10 glucose molecule ( more branches, short branched)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
94
Q

similarities between amylopectin and glycogen

A

alpha glucose 1,4 and alpha glucose 1,6 glycosidic bond, polysaccharide/polymer/insoluble, bulky

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
95
Q

differences between amylopectin and and glycogen

A

amylopectin is stored as grains, and branches are less branched, long branches.
glycogen is stored as granules and branches are many short btanches

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
96
Q

cellulose short

A

beta glucose beta 1,4 glycosidic bond, unbranched

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
97
Q
A

cellulose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
98
Q

why each glucose molecule is rotated 180degrees in cellulose

A

to prevent helix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
99
Q

—-

A

hydrogen bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
100
Q

fibers contain

A

hydrogen bonds and microfibres

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
101
Q

microfibres contain

A

60-70 cellulose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
102
Q

in order to maintain beta 1,4 glycosidic bonds in cellulose

A

each succesive glucose molecule is rotated 180 degrees to prevent the formation of helix( cellulose is a part of cell wall so it cannot be in the form of a helix)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
103
Q

hydrogen bonds in cellulose

A

is formed between 2 cellulose chains, invidual hydrogen bond is weak but many hydrogen bonds together form high tensile strength about 60-70 cellulose molecule become tightly cross linked to form microfibrils are in turn held together in bundles called fibre. hydrogen bonds join 5 microfibrils together

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
104
Q

importance of hydrogen bonds in cellulose

A
  • provide high tensile strength
  • holds the chains together
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
105
Q

how is the structure of cellulose adapted for its function?

A

1) each succesive glucose molecule is rotated 180*, it keeps the molecule straight, prevents the formation of helix
2) cellulose is unbranched linear polymer allowing it to lie parallel to each other with many OH groups projecting in different direction to form hydrogen bond, it provides intensive strength to withstand turgor pressure and prevents the cell from bursting
3) arrangement of fibre around the cell help in maintaining the shape of the cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
106
Q

similarities between starch, cellulose and glycogen

A

polysaccharide, polymer and insoluble

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
107
Q

starch bond

A

alpha glucose 1,4 and alpha glucose 1,6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
108
Q

glycogen bond

A

alpha glucose 1,6 and alpha glucose 1,4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
109
Q

cellulose bond

A

beta glucose 1,4 glycosidic bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
110
Q

starch function

A

storage

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
111
Q

glycogen function

A

storage

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
112
Q

cellulose function

A

structural

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
113
Q

starch branch

A

only amylopectin branched

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
114
Q

glycogen branches

A

branched

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
115
Q

cellulose branches

A

unbranched

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
116
Q

starch is present in

A

chlorophlast

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
117
Q

glycogen is present in

A

muscle and liver

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
118
Q

cellulose is present in

A

cell wall

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
119
Q

starch is present as

A

grains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
120
Q

glycogen is present as

A

granules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
121
Q

cellulose is present as

A

fibre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
122
Q

starch orientation

A

same

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
123
Q

glycogen orientation

A

same

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
124
Q

cellulose orientation

A

each succesive glucose is rotated 180 degrees

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
125
Q

importance of being branched

A
  • compact
  • occupy less space
  • quickly hydrolysed
  • insoluble- no osmotic change
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
126
Q

starch monosaccharide

A

alpha glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
127
Q

glycogen monosaccharide

A

alpha glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
128
Q

cellulose monosaccharide

A

beta glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
129
Q

differences between the structure of deoxyribose and the ring structure of alpha glucose

A

alpha glucose is a pyranose ring and deoxyribose sugar has a furanose ring, alpha glucose has 6 carbons and deoxyribose has 5 carbons, 5 OH bonds in alpha glucose , bond formed between 1st and 5th carbon atoms in alpha glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
130
Q

advantages for a mammal having a storage molecule that is highly branched

A

many ends for attachement of glucose, can be stored quickly, makes it more compact, occupies less space

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
131
Q

2 structural differences between fructose and sucrose

A

1) fructose is a monosaccharide and sucrose is a disaccharide
2) fructose has no glycosidic bonds and sucrose has glycosidic bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
132
Q

color of iodine solution in the presence of starch

A

blue-black

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
133
Q

describe how a hydrogen bond is formed

A

hydrogen bond is formed between oxygen and hydrogen atom. oxygen has a slight negative charge and hydrogen has an electro positive charge.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
134
Q

what would happen to the iodine- amylose complex if the solution was heated at 60 degrees celsius

A

hydrogen bond breaks, colour remains orange brown, looses helix structure, iodine not trapped

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
135
Q

number of different types of amino acids

A

20

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
136
Q

every amino acid has

A
  • 1 amine group
  • R group
  • carboxylic acid
  • hydrogen
    all attached to same carbon
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
137
Q
A

amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
138
Q
A

formation of peptide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
139
Q

number of peptide bonds

A
  • number of peptide bond is = n-1, when n is the number of amino acids
  • peptide bond is not broken by adding water at room temperature
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
140
Q

zwitter ions

A

amino acid when dissolved in water form zwitter ions ( have positively and negatively charged groups or amphoteric)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
141
Q
A

zwitter ions

142
Q

Examples of proteins

A
  • all enzymes are proteins
  • some hormones, for example: insulin, glycine
  • protection, examples: antibodies, fibrinogen, thrombin and fibrin
  • contractile ( present in muscle ) example: myocin and actin
143
Q

structural proteins

A

collagen and keratin

144
Q

transport proteins

A

hemoglobin, myoglobin, and carrier proteins

145
Q

homeostasis

A

some proteins act as a buffer to maintain the PH

146
Q

properties determined by R group

A
  • physical and chemical properties of an amino acid
  • bonds can be formed between amino acids which help in folding, solubility, and polarity (charge).
  • if an amino acid contains a polar R group, it can form a hydrogen bond, and the amino acid is considered to be soluble.
147
Q

types of structures of proteins

A

primary structure, secondary structure, tertiary structure and quaternary structure

148
Q

primary structure

A

linear sequence of amino acids joined by peptide bonds to form a polypeptide. change in the primary structure changes the property of protein, change in primary structure affects all levels of proteins

149
Q
A

primary structure
the line is a peptide bond and the ends have NH2 and COOH

150
Q

secondary structure : α helix

A

undergoes folding to give a secondary structure which is maintained by hydrogen bond. hydrogen bond formed between the first and 4th oxygen in the carboxyl group, C=O of the first amino acid, and hydrogen in the NH group of amino acids four down the chain, pattern of bonding pulls the polypeptide chain into a helical structure, each helix contains 3.6 amino acids R group of amino acid projects outward where they are free to interact

151
Q
A

alpha helix diagram

152
Q

secondary structure : β pleated sheet

A

2 or more segment of the same poly-peptide chain lined up next to each other, form a sheet-like structure held by a hydrogen bond, R group extend above or below the plane of a sheet.

153
Q
A

beta pleated sheet diagram

154
Q
A

beta pleated sheet structural chain

155
Q

in secondary structure R group

A

projects out

156
Q

tertiary structure

A

formed due to interaction of R groups, 3D in nature, allow distant amino acid to be closer to each other, due to folding and interaction between R group,

157
Q

hydrogen bond

A

formed between electropositive and electronegative atoms, weak bonds can be broken by increasing temperature and change in PH

158
Q

bond formed that common for tertiary and quaternary structure

A

hydorgen and ionic and disulphide

159
Q
A

hydrogen bond

160
Q

ionic bond

A

formed between oppositely charged ions at a particular PH. change in the PH breaks ionic bond

161
Q
A

ionic bond

162
Q

disulfide bond

A

formed between 2 cysteine, covalent bond, strongest bond, last bond to break, can be broken by increasing the temperature

163
Q
A

disulphide bond

164
Q

strength of bond ( decreasing strength)

A

1) disulphide
2) ionic
3) hydrogen

165
Q

hydrophobic interaction

A

interaction between 2 nonpolar R groups. wander waals force: non specific attractive force between 2 groups that are very close to each other

166
Q
A

hydrophobic interaction

167
Q

quaternary structure is made up of more than

A

one poly-peptide chain

168
Q

primary -> secondary

A

folding/ coiling

169
Q

primary features

A

1 poly peptide , peptide bond

170
Q

secondary features

A

1 polypeptide and hydrogen bond

171
Q

tertiary features

A

1 polypeptide, interaction of R groups, 3D, hydrogen and ionic and disulphide bond, hydrophobic interaction

172
Q

quarternary features

A

more than 1 polypeptide, hydrogen, ionic, disulfide, hydrophobic

173
Q

shapes of globular

A

spherical

174
Q

shapes of fibrous

A

long narrow fibre

175
Q

solubility of globular

A

soluble in H2O

176
Q

solubility of fibrous

A

insoluble in H2O

177
Q

stability of globular

A

unstable

178
Q

stability of fibrous

A

stable

179
Q

durability of globular

A

sensitive to change

180
Q

durability of fibrous

A

less sensitive

181
Q

sequence of amino acids in globular

A

regular in temperature and PH

182
Q

sequence of amino acids in fibrous

A

irregular in temperature and PH

183
Q

Purpose of globular

A

functional

184
Q

Purpose of fibrous

A

structural

185
Q

example of globular

A

enzymes, hemoglobin, antibodies

186
Q

example of fibrous

A

collagen

187
Q

globular

A

proteins which are spherical, soluble in water, hydrophilic R group outside, and hydrophobic R group inside

188
Q

hemoglobin

A

quarternary, 4 polypeptide chains ( 2 alpha and 2 beta-globin ), globular, each polypeptide chain contains 1 haem/Fe2+/prosthetic group (non-protein component) 2 genes required to make hemoglobin, each polypeptide chain contains 1 haem so 4 haem group in hemoglobin

189
Q

1 Fe2+ carries 1 molecule of oxygen =

A

4 molecules of O2, 8 atoms of O2 carried by hemoglobin molecule. chains are arranged in a way that the hydrophobic R group is facing inside and the hydrophilic R group pointing outside ( towards cytoplasm) this makes the hemoglobin soluble

190
Q
A

hemoglobin is arranged towards the cell membrane so that it decreases diffusion distance

191
Q

loading of O2 in

A

alveoli

192
Q

unloading of O2 in

A

tissue

193
Q

CO + hemoglobin ->

A

carboxyhemoglobin (the most stable, permanent, binding, irreversible)

194
Q

O2+ hemoglobin ->

A

oxyhemoglobin ( reversible)

195
Q

CO2 + hemoglobin ->

A

carbaminohemoglobin ( reversible)

196
Q

CO and O2 share

A

the same binding site ( heam)

197
Q

CO2 binds to the

A

polypeptide chain

198
Q

affinity

A

CO, O2, CO2 ( decreasing order of affinity)

199
Q

collagen

A

fibrous, quarternary , 3 polypeptide

200
Q

collagen is present in

A

skin, walls of blood vessels, ligament, tendon

201
Q

3 poly peptides coil together to a

A

triple helix which is a collagen molecule

202
Q

triple helix which is a collagen molecule has

A

hydrogen bonds

203
Q

triple helix has

A

staggered and has covalent bonds

204
Q

order of amino acids

A

glycine, proline, arginine/hydroxyproline

205
Q
A

glycine formula

206
Q

why is glycine present in every 3rd position?

A
  • simplest amino acid with a small R group when compared with other amino acids, it allows the 3 polypeptide chain to lie closer to each other and form a triple helix
  • triple helix is arranged in parallel rows and have stagered ends
  • in between the collagen molecule, covalent bonds are present, collagen bonds join to form fibrils which in turn form fibre
207
Q

how is the structure of collagen adapted for its function?

A

presence of hydrogen bonds and covalent bonds between collagen molecule form high tensile strength. it helps to withstand high pressure/pulling forces

208
Q

differences between hemoglobin and collagen

A

hemoglobin is globular whereas collagen is fibrous
hemoglobin has 4 polypeptide and collagen has 3 polypeptide
hemoglobin function is carries O2 and collagen function is high tensile strength

209
Q

biuret test

A

takes 2cm3 of sample, to it add KOH ( changes PH, ionic and hydrogen bond breaks) add 2cm3 of CuSO4, blue -> lilac

210
Q

adaptations of cellulose

A

Presence of gaps between microfibrils allows solute to reach cell membrane and makes cell wall fullypermeable.

211
Q

lipids

A
  • less oxygen when compared to carbohydrates
  • releases more energy, ( has many C-C and C-H breaking in which releases a lot of energy )
  • insoluble in water but soluble in organic solvent ( alcohol)
212
Q

triglyceride

A

glycerol + 3 fatty acids

213
Q
A

glycerol structure

214
Q

glycerol

A
  • polar
  • water soluble
  • triol -3OH-
  • hydrophillic
215
Q

saturated fatty acid

A

C-C single bond
solid at room temperature
animal source
it shows the tendency to stick to each other and to the walls of arteries

216
Q

unsaturated fatty acid

A
  • C=C or C≡C
  • liquid at room temperature
  • plant source
  • hydrogenation - excess of converting unsaturated fatty acids to a saturated fatty acid by the addition of H2
217
Q
A

formation of triglyceride

218
Q

glycerol is linked to fatty acids by

A

ester bond

219
Q

as the polar group of glycerol and fatty acids are lost during

A

condensation , triglyceride produced is non polar and its insoluble in H2O

220
Q

examples of lipids

A
  • fats and oils
  • phospholipid
  • wax
  • steroid
221
Q

fats and oils functions

A

energy reserve

222
Q

phospholipid function

A

cell membrane

223
Q

wax function

A

waterproofing surface of plant leaf

224
Q

steroids function

A

horomones

225
Q

how is triglycerides adapted for its function

A
  • has many C-C and C-H bonds breaking up of these bonds releases energy
  • fats stored under the slom of adipose tissue acts as an insulator
  • blubber: present in sea mammals helps in bouncy acts as an insulating layer
  • metabolic source of water in animals living in desert, triglyceride is oxidised to release water
226
Q
A

phospholipid

227
Q

phospholipid head is

A

hydrophilic

228
Q

phospholipid tail is

A

hydrophobic

229
Q

one fatty acid chain is replaced with

A

phosphate group in phospholipids

230
Q

phospholipid contains

A

charge/ polar so its soluble/hydrophillic

231
Q

head of phospholipid is made up of

A

glycerol + phosphate group

232
Q

tail is

A

nonpolar/ hydrophobic ( made up of 2 fatty acid chains)

233
Q

phospholipid is present as a bilayer in the cell membrane with

A

hydrophillic head pointing outward and hydrophobic tail inside

234
Q

the hydrophobic chain makes the cell membrane

A

selectively permeable allows only fat soluble materials to pass through it

235
Q

water

A

hydrogen bond is present between 2 water molecules

236
Q

properties of water

A

1) polarity
2) high surface tension and cohesion
3) density and freezing points
4) neutral
5) high water capacity

237
Q

polarity description

A

uneven distribution of chargers over a molecule

238
Q

importance of water being polar

A

1) allows water to be a solvent
2) water as a transport medium

239
Q

how does polarity allow water to be a solvent

A

molecules that have groups with dipoles are said to be polar, they are attracted to water molecules, because the water molecules also have dipoles, such molecules are said to be hydrophilic (water-loving), and they tend to be soluble in water. molecules that do not have dipoles are said to be non-polar, example: lipids, are not attracted to water and they are hydrophobic (water-hating). such properties make possible the formation of plasma membranes

240
Q

how does polarity help water as a transport medium

A

water is the transport medium in blood, in the lymphatic excretory and digestive systems of animals, and in the vascular tissues of plants, here again its solvent properties are essential

241
Q

high surface tension and cohesion description

A
  • water molecules have very high cohesion, in other words, they tend to stick to each other
  • high surface tension: at the surface of a liquid a force called surface tension exists between molecules as a result of cohesive forces between molecules. this force makes the surface occupies the least possible surface area
242
Q

importance of high surface tension and cohesion

A

1) this is the reason for the way water moves in long, unbroken columns through the vascular tissue in plants and is an important property in cells
2) high cohesion also results in high surface tension at the surface of the water, this allows certain small organisms, such as the pond skater, to exploit the surface of the water as a habitat. allowing them to settle on or skate over its surface

243
Q

density and freezing properties description

A

water is an unsual chemical because the solid form, ice is less dense that its liquid form . below 4°C the density of water starts to decrease, ice therefore floats on liquid water and insulates water under it

244
Q

density and freezing properties importance

A

this reduces the tendency for large bodies of water to freeze completely, and increases the chances of life surviving in cold condition
changes in the density of water with temperature cause currents to help to maintain the circulation of nutrients in the ocean

245
Q

neutral description

A

PH=7

246
Q

nuetral importance

A

suitable PH for living cells

247
Q

high water capacity description

A

it is the amount of heat required to raise the temperature of 1Kg of water by 1°C
as hydrogen bonding restricts the movement of water molecules, a relatively large amount of energy is needed to raise the temperature of water

248
Q

high water capacity importance

A

this means that large bodies of water such as oceand and lakes are slow to change temperature as environmental temperature changes, as a result they are more stable habitats
due to the high proportionation of water in the body internal changes in the temperature are also minimized , making it easier to achieve stable body temperature

249
Q

the high heat of vaporization description

A

it is the amount of heat needed to vaporize a liquid

250
Q

high heat of vaporization importance

A

since a relatively large amount of energy is needed to convert water to gas, the process of evaporation transfers a correspondingly larger amount of energy and can be an effective means of cooling the blood, as in sweating and panting conversely, a relatively large amount of energy must be transferred from water before it is converted from a liquid to solid ( ice), this makes it less likely that water will freeze an advantage both for the bodies of living organisms and for organisms which live in water, i.e. large amount of heat can be lost with minimal loss of water from the body(cooling effect)

251
Q

biological functions of water in all organisms

A

structure- high water content of cells( 70-95% )
solvent and medium for diffusion
reagent in hydrolysis

252
Q

biological functions of water in plants

A

osmosis and turgidity ( important in many ways, such as growth, cell enlargement, support, guard cell mechanism)
reagent in photosynthesis
translocation of inorganic ions and organic compounds

253
Q

biological functions of water in animals

A

transport in the blood vascular system, lymphatic system, excretory system
osmoregulation
cooling by evaporation, such as sweating

254
Q

what will break an ionic bond between amino acids?

A

ph change, not high temperature

255
Q

how many dipeptides can be assembeld from 12 amino acids?

A

12^2 = 144

256
Q

function of iron in hb

A

binds oxygen to hb molecuke

257
Q

min no of c atoms in an amino acid?

A

two

258
Q

which have properties dependent on hydrogen bonds?

A

cellulose, hb and water

259
Q

which features result in collagen having high tensile strength?

A
  1. covalent bonds between adjacent molecules
    bio post pp notes 6
  2. each 3 stranded molcule is held together by hydrogen bonds
  3. r group of every 3rd amino acid is small insoluble nature is irrelevant!
260
Q

when ph is low, some enzymes don’t function properly as their 3d shape
gets changed. what explains the change in 3d shape?

A

h+ ions attach themselves to negatively charged r groups

261
Q

peptide bond is a

A

covalent bond

262
Q

disulphide bond is the

A

the strongest/ last to break

263
Q

carboxyl group is

A

COOH

264
Q

n is the number of amino acids, number of peptide bonds would be

A

n-1

265
Q

in the formation of a peptide bond

A

one amino acid loses oh group from
cooh

266
Q

both hydrogen and ionic bonds are

A

weak bonds

267
Q

when primary structure changes

A

all subsequent structures change as
well

268
Q

glucose has c

A

=o

269
Q

antibodies are made of

A

two polypeptides

270
Q

glycine has a small

A

r group

271
Q

hb changes shape as

A

oxygen loads

272
Q

collagen is insoluble in

A

water

273
Q

collagen is a repeat sequence of

A

3 amino acids

274
Q

there is no branching in

A

proteins

275
Q

hb and collagen always contain atleast

A

4 double bonds even

276
Q

during protein denaturation,

A

tertiary structure of enzyme is lost / affected
(happens when extreme ph yk)

277
Q

ionic bond in secondary >

A

peptide bond in secondary (in those venn
diagram qs)

278
Q

large increases in temp dont increase

A

hydrophobic interactions

279
Q

disulphide maintains both

A

tertiary and quarternary structure

280
Q

peptide bond can’t be broken down by hydrolysis at

A

room temperature

281
Q

any side chain binding at the site of the R group needs to have

A

a carbon atom which can form a bond

282
Q

if different regions form a 3d shape

A

it is tertiary!!

283
Q

which property of water allows insects to stand on the surface of ponds?

A

cohesion between water molecules
ability to form hydrogen bonds with other molciles
*other properties are honestly irrelevant

284
Q

which property of water minimises temperature changes in cells &
organisms?

A

specific heat capacity only
^preference over lov ig

285
Q

as a frozen lake warms after a cold winter, mineral nutrients are brought
to surface. whyyyyy

A
  1. water’s greatest density is at 4 C
  2. water is a solvent
    high shc and hydrogen bonds are *irrelevant
286
Q

why may fish living in ponds survive temperatures below 0 C in winter?

A

ice on pond surface insulates the water in the pond
properties of water needed for fish to survive: high thermal capacity, max
density at 4 C

287
Q

which feature of water is least likely to affect the life of an animal in a
tropical rain forest?

A

maximum density at 4 C
^water won’t freeze in a tropical rain forest so this property is irrelevant
as a whole

288
Q

which property of water is important in transpiring plants to prevent
enzymes in leaves from being denatured?

A

t retains a lot of heat to evaporate = high lov [due to presence of h
bonds]
[amount of energy to make liq to gas is high]
[IRRELEVANT] it retains a lot of heat (does not mean shc, shc is when it
requires a high amount of heat for a change in temperature)

289
Q

what processes in plants is hydrogen bonding important on hot sunny
days?

A

anything that prevents water loss
allowing leaves to cool down at night = more water loss (?) - so its wrong

290
Q

processes based on h bonding

A

everythign except solvent i think
1. temp control due to evaporation
2. provides constant env for aquatic organisms

291
Q

in unsaturated lipid molecules, where are double bonds located?

A

within fatty acids only

292
Q

the beetroot qs (red pigment cannot pass out of cells)

A

in ethanol, phospholipids dissolve so pigment passes out
in dilute hcl, protein denatures so pigment passes out

293
Q

unsaturated —> saturated fats / what property of fats has changed?

A

their hydrocarbon chain will fit together more closely
extra: uns are liquids at room temp and s are solids!

294
Q

trigylcerides have a LOWER ratio of oxygen to carbon than

A

carbohydrates (this is also the reason they release greater amounts of
energy!)

295
Q

trigylcerides are

A

hydrophobic

296
Q

non-polar fatty acid chains can be attracted to

A

each other by
hydrophobic interactions

297
Q

function of triglycerides is like

A

energy storage mainly

298
Q

which juice contains the greatest mass of non-reducing sugars?

A

mass of ppt before hydrolysis is due to reducing sugars! so substract the
mass before and after to get mass of non-reducing sugars
mass of ppt directly proportional to mass of reducing sugar

299
Q

when its just reducing sugars, you can use either the reducing or non
reducing test cuz it doesnt make a diff

A

add hydrolytic enzyme and heat w benedicts
boil w hcl, neutralize and then heat w benedistcs
NOT - dissolve in water, neut and then heat LMAOO

300
Q

which may contain non reducing sugars?

A

when there’s a diff in intensity of color in the reducing and non-reducing
sugar tests ykwim

301
Q

[cellulose related] what is the significance of the fact that the oh groups
on carbon 2 in adjacent glucose molecules are on opposite sides of the
molecule?

A

they can form hydrogen bonds with adjacent oh and ch2oh groups
of other cellulose molecules

302
Q

semi-quantitative test

A

provides indication of relative concentrations
color of solution approximately tells u conc of rs (benedicts is a sq test)

303
Q

the working of a colorimeter

A

colored solution = less light transmitted when compared to colorless
solution
less light transmitted = more light absorbed
as intensity of color increases, absorbance increases!
y axis will be absorbance

304
Q

serial dilution =

A

solution reduces by a percentage of the previous
solution

305
Q

when an enzyme is present

A

biuret test will give a purple color

306
Q

only reactions where there is an obvious color change can be
investigated using a

A

colorimeter

307
Q

no solid particls formed during

A

benedict’s test

308
Q

triglycerides are not suited for cell surface membrane cuz

A

no phosphate
polar group; cant form hydrogen bonds with water; cant form bilayer

309
Q

triglycerides > carbs cuz

A

less mass needed to provide same energy /
low(er) mass to energy ratio

310
Q

mention that water is

A

dipolar

311
Q

mportancd of water as a solvent in plants

A
  1. dissolves ions and minerals and named polar substances
  2. transport of solutes through xylen
  3. storage of solutes in vacuole
  4. metabolic reactions occur in water
312
Q

peptide bond is stronger than any

A

tertiary structure bond

313
Q

unless specific amino acid chain given

A

primary structure can’t be seen

314
Q

secondary

A

areas of random arrangements are shown

315
Q

tertiary:

A

3d / globular / interaction of r groups / folding of polypeptide
chain or secondary structure

316
Q

globular proteins can have

A

quarternary structure also

317
Q

triglycerides have a large

A

mass per unit volume (more energy released)

318
Q

if a specific protein is mentioned

A

go over its functions and type first (for
example, if collagen is mentioned, say fibrous / structural function

319
Q

fats over carbs?

A

lower mass to energy ratio
higher carbon to hydrogen ratio (more ch bonds)

320
Q

polysac over glucose?

A

glucose is a reactive molecule
glucose would lower water potential
compact and insoluble points (give preference to these 2)

321
Q

description of bonds

A

h bonds bwtween polar groups (co and nh)
ionic bonds between ionised amine and carboxylic acid groups
hydrophobic interactions between non polar side chains
disulphide between cysteine (s-h) groups
*when they ask to explain tertiary mention folding/coiling

322
Q

state why tri and phospholipids cannot be described as polymers

A

not composed of monomers / repeating subunits

323
Q

define polymer

A

macromolecule made up of many repeated subunits called monomers

324
Q

h bonds dont stabilise mrna cuz

A

mrna is single stranded (no helix)

325
Q

hb contains

A

nitrogen it seems

326
Q

dna contains

A

phosphate it seems

327
Q

phospholipids and antibodies contain

A

nitrogen

328
Q

high lov

A

water is liquid over a wide range of temperatures

329
Q

dna has a loose helix

A

/ collagen has a tightly coiled helix

330
Q

secondary structure has a regular order/pattern based

A

on h bonds
between co group of one amino acid and nh group of another

331
Q

proteins / amylose can form

A

helical structures (glycogen cannot form
helical structure)

332
Q

hydrophilic means it can form h bonds with

A

water

333
Q

for ser, its fluid filled channels or sacs NOT

A

flattened

334
Q

phospholipids may have nitrogen / or an additional group like

A

choline

335
Q

globular proteins are water soluble

A

can form h bonds w water

336
Q

enzymes are

A

macromolecules

337
Q

If glucose is hydrolysed and boiled with Benedict’s solution

A

it tests negative

338
Q

: Enzymes do NOT have

A

quaternary structure

339
Q

Peptide bond is the last to break as temperature of enzyme is increased

A

Next is disulphide.

340
Q

Tertiary structure maintain globular shapes of

A

enzyme

341
Q

When 2 cysteine amino acids join

A

they are held together by peptide bonds only

342
Q

Find out the wrong statement. What occurs during protein denatured by pH change

A

Breaking of peptide bonds leads to loss of active site - incorrect
Disruption of ionic bond b/w amino R groups - correct
Loss of alpha helix b/w amino acid - correct
Loss of tertiary structure which causes loss of function - correct.

343
Q

What level of protein structures are always involved when competitive and noncompetitive inhibitors bind to enzymes?

A

Competitive and noncompetitive: tertiary structure

344
Q

Explain how amino acids can be close together in an active site by explaining structure of protein.

A

Further coiling and folding of polypeptide chain
Giving tertiary structure
Held in position by R group interaction
Brings distant amino acid close

344
Q

Globular proteins always have

A

hydrophilic amino acids to towards the outside and hydrophobic amino acids towards the inside

345
Q

Explain role of H bonds in maintaining secondary structure:

A

H bonds maintain the alpha helix and beta pleated sheet

346
Q

Describe the hydrogen bonding that occurs between water molecules

A

Hydrogen bond is a weak bond between oxygen atom of 1 H2O molecule and the hydrogen atom of another H2O molecule
Oxygen is highly electronegative more than H
Oxygen has two lone pairs so it can form 2 hydrogen bonds
Asymmetrical electron distribution
Oxygen has delta - and hydrogen has delta + charge

347
Q

What is the effect of replacing glutamine (polar) with valine (non-polar) in alpha/beta globin?

A

Glutamine is polar and valine is non-polar
Change in tertiary shape
Change in quaternary structure of haemoglobin
Haemoglobin less soluble
Haemoglobin is less efficient at
transporting oxygen

348
Q

Explain role of H bonds in maintaining tertiary structure:

A

H bonds stabilise further folding of polypeptide
Between R groups with amine and carboxyl groups
Helps maintain globular shape, 3D shape

349
Q

Function of collagen in the wall of arteries:

A
  1. withstands pressure ;
  2. prevents, overstretching / AW ;
  3. prevents, bursting
350
Q

Structure of collagen vs. Haemoglobin:

A
  1. 1 polypeptides are not identical (v. 2 identical, α / β, polypeptides) ;
  2. triple helix or three, polypeptides / helices (v. 4 polypeptides) ;
  3. only composed of amino acids or no, prosthetic group / haem / iron ;
  4. (fibrous so) not globular ;
  5. no complex folding / AW (v. complex folding) ; A no tertiary structure
  6. glycine is repeated every 3rd position / more glycine ;
  7. repeating triplets of amino acids / large number repeating amino acid sequences (v. greater variety) ;
  8. AVP ; e.g. different primary structure / AW
  9. variation in amino acid sequences (v specific sequences)
  10. all polypeptides, helical / AW (v. α different to β, polypeptides)
  11. hydrogen bonds tussen polypeptides (v. Van der Waals)
  12. covalent bonds between molecules (to form fibrils) (v. none)
  13. 300 nm long polypeptides (v 5–10nm)
  14. each polypeptide over 1000 amino acids (each 141 / 146 amino acids)
351
Q
A

9700 (14 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions