own notes c,l,p Flashcards

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1
Q

what are carbohydrates?

A

organic compounds made up of c,h,o–(made up of simple sugars a&B)?

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2
Q

name 4 examples of carbohydrates

A

glucose, glycogen, starch, cellulose

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3
Q

what are carbohydrates made of

A

1 c, 2h, 1o

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4
Q

what are 3 uses of carbohydrates

A
  1. storage for energy
  2. source of energy
  3. structural units
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5
Q

what are the 3 groups of carbohydrates?

A

monosaccharides
disaccharides
polysaccharides

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6
Q

describe monosaccharides

A
  • simplest single sugars- simplest carbohydrate
    -used as a source of energy
    -sugars which taste sweet
    -soluble in water
  • same number of c as o
    -form white crystalline solids
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7
Q

3 examples of monosaccharides

A

fructose, galactose, glucose(C6H12O6)

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8
Q

what are monosaccharides are they monomers

A

monomers of more complex carbohydrates- bond to form disaccharides or polysaccharides

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9
Q

what are the two isomers ( forms) of glucose?

A

a-glucose and b-glucose

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10
Q

what are 4 types of monosaccharides?

A

a-glucose, b-glucose, ribose, deoxyribose

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11
Q

what are isomers?

A

molecules with the same formula, but whose atoms are arranged differently in space eg a-glucose and b-glucose.

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12
Q

what’s a glyosidic bond?

A

a bond formed between two monosaccharides by a condensation reaction

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13
Q

(ud)what does a-glucose form?

A

starch and glycogen

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14
Q

(ud) what does b-glucose form?

A

cellulose

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15
Q

how are disaccharides formed?

A

when two monosaccharides are joined together a condensation reaction occurs to produce a glyosidic bond

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16
Q

what are the three most common disaccharides

A

maltose (reducing s), sucrose (non-reducing s) and lactose (reducing s)

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17
Q

how are disaccharides broken into monosaccharides

A

by a hydrolysis reaction which requires addition of water

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18
Q

what is the -OH group

A

the hydroxyl group

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19
Q

if both monosaccharides are a-glucose, what bond do they form?

A

a 1-4 glyosidic bond .

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20
Q

examples of making disaccharides:
a-glucose+a-glucose=…

A

maltose

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21
Q

examples of making disaccharides:
a-glucose+fructose=…

A

sucrose

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22
Q

examples of making disaccharides:
a-glucose+b-glucose=…

A

lactose

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23
Q

examples of making disaccharides:
b-glucose+b-glucose=…

A

cellobiose

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24
Q

what is ATP

A

energy currency of a cell

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25
Q

what are polysaccharides?

A

polymers of monosaccharides, made of many monosaccharides joined together.

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26
Q

3 examples of polysaccharides…

A

starch, glycogen, cellulose

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27
Q

what are polysaccharides good as ( examples too)

A

they are good energy stores- glycogen in animals, starch in plants.

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28
Q

how do polysaccharides hold glucose and how is this useful?

A

hold glucose molecules in chains, so they can easily be snipped off by hydrolysis when required for respiration ( sped up with enzyme)

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29
Q

is amylose( dk what type/ where from) branched or unbranched?

A

unbranched

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30
Q

is amylopectin and glycogen branched or unbranched?

A

branched

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31
Q

amylopectin and glycogen are branched, what does this mean for them?

A

more compact and offer the chance for lots of glucose molecules to be snipped by hydrolysis at the same time when lost of energy is required quickly.

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32
Q

why are polysaccharides less soluble in water than monosaccharides?

A

due to their size and regions which could hydrogen bond in water are hidden.

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33
Q

what would happen if many glucose molecules did dissolve in the cytoplasm?

A

the water potential would reduce so excess water would diffuse in, disrupting the normal workings of the cell.

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34
Q

what is the most common polysaccharide

A

starch

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35
Q

where is cellulose found & describe it.

A

found in plants, forming cell walls- tough insoluble fibrous substance

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36
Q

what’s a homopolysaccharide ?

A

polysaccharide made up of one type of monosaccharide

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37
Q

what’s a heteropolysaccharide?

A

polysaccharide made up of more than one type of monosaccharide

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38
Q

cellulose is a homopolysaccharide, what is it made of?

A

made up of b-glucose molecules bonded by condensation reactions to form glyosidic bonds
(chains are straight and lie side by side ( dont spiral)

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39
Q

sate key ideas about cellulose

A

polysaccharide
chains of b-glucose
are straight( don’t spiral)

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40
Q

cellulose^^ what helps the chain from spiralling

A

every other b glucose molecule is rotated 180 degrees

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41
Q

what does the hydrogen bonding between the rotated b-glucose molecules in each chain do?

A

gives the chain additional strength, and stops it from spiralling.

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42
Q

cellulose: what enables the hydrogen bonds to be formed between chains

A

the hydroxyl group on carbon 2

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43
Q

what are lipids made up of

A

large amounts of carbon and hydrogen and smaller amounts of oxygen.

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44
Q

are lipids insoluble in water? why?

A

yes as they are not polar

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45
Q

what are lipids made up of (atoms)

A

large amounts of carbon and hydrogen and smaller amounts of oxygen.

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46
Q

are lipids insoluble in water? why?

A

yes as they are not polar- they dissolve in alcohol

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47
Q

what are the three most important lipids?

A

triglycerides, phospholipids, steroids (all macromolecules)

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48
Q

what is a triglyceride made up of?

A

1 glycerol and 3 fatty acids

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49
Q

state what glycerol has

A

3 -OH groups
=its an alcohol

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50
Q

what do fatty acids have?

A

-have a carboxyl group (-COOH)
attached to a hydrocarbon tail

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51
Q

what can the carboxyl group do?

A

ionise H+ and -COO- group thus an acid

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52
Q

what does a saturated fatty acid have

A

no c=c bonds

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53
Q

what does an unsaturated fatty acid have

A

c=c bonds

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54
Q

what does a single c=c bond mean (in terms of name)

A

its monounsaturated e.g. oleic acid

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55
Q

what does more than one c=c bond mean (in terms of name

A

its polyunsaturated e.g. linoleic acid

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56
Q

what does having more than one c=c bond do ***

A

changes the shape of the hydrocarbon chain (gives it a kink)

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57
Q

what does a kink in the hydrocarbon chain do

A

kink pushes molecules apart making them more fluid , if there are more unsaturated fatty acids, mp is lower.

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58
Q

what reaction forms a triglyceride and what happens

A

a condensation reaction occurs (h20 produced) between the -COOH group (fatty acid) and the -OH (glycerol)

59
Q

what is the covalent bond formed between the glycerol and fatty acid called

A

an ester bond

60
Q

what are the 5 functions of triglycerides

A
  1. energy source
  2. energy store
  3. insulation
  4. buoyancy
    5.proctection
61
Q

how does a triglyceride act as an energy source

A

broken doen in respiration to release energy & generate ATP . broken into CO2 and H2O

62
Q

how does a triglyceride act as an energy store

A

insoluble in water so doesn’t affect water potential

63
Q

how does a triglyceride act as an insulator

A

adipose tissue=storage location for lipid/blubber

64
Q

what type of bond is an ester bond

A

a covalent bond

65
Q

how does a triglyceride aid buoyancy

A

fat is less dense than water so mammals stay afloat

66
Q

how does a triglyceride act as protection

A

fat is around delicate organs- shock absorber.
bacteria covered in lipid

67
Q

what is a phospholipid

A

same as a triglyceride but 1 fatty acid replaced with a phosphate group

68
Q

talk about the fatty acids in phospholipids

A

fatty acids found here have an even number of hydrocarbon chains-commonly 1 saturate and 1 unsaturated

69
Q

phospholipids: when surrounded by water what does the phosphate group have?

A

has a negative charge thus polar

70
Q

phospholipids: are fatty acid tails polar or non polar

A

non-polar

71
Q

phospholipids: what property does the head have

A

hydrophillic

72
Q

phospholipids: what property does the tail have

A

hydrophobic

73
Q

phospholipids: if they are hydrophobic and hydrophilic, they are…

A

amphipathic

74
Q

what may phospholipids form on the surface of water

A

a layer- heads in tails out
or micelles (tiny balls)

75
Q

what are phospholipids great at forming?

A

forming membranes around cells and organelles (phospholipid bilayer)

76
Q

cholesterol is a ______

A

lipid

77
Q

state necessary things about cholesterol

A

-its a steroid alcohol
-not made of glycerol or fatty acids
-consists of 4 carbon based rings or isoprene units
-small and hydrophobic
- can sit in the middle of the hydrophobic bilayer
-regulates the fluidity of the membrane

78
Q

where is cholesterol made

A

in the liver of animals

79
Q

what does stigmasterol have (found in plants)

A

has a double bond between carbon 22 & 23

80
Q

what are steroid hormones made of

A

cholesterol

81
Q

can steroid hormones pass through the hydrophobic cell memebrane?

A

yes because small and hydrophobic

82
Q

where are steroid hormones abundant

A

in plants

83
Q

how do you identify lipids and what’s a positive test

A

emulsion test-white layer on top

84
Q

what elements are present in lipids

A

O,H,C

85
Q

what elements are present in proteins

A

C,H,O,N,S

86
Q

what are peptides made of?

A

made of amino acid molecules joined by peptide bonds

87
Q

what are the 4 protein structures

A

primary, secondary, tertiary, quaternary

88
Q

what are amino acids

A

monomers of all proteins, all amino acids have the same basic structure

89
Q

whats a peptide bond

A

a bond formed when two amino acids are joined by a condensation reaction

90
Q

what are proteins

A

large polymers comprised of long chains of amino acids. the properties of proteins give them a variety of functions.

91
Q

3 functions of proteins:

A
  • form structural components of animals (muscles)
    -their tendency to adapt to specific shapes makes proteins important as enzymes, antibodies and some hormones
    -membranes have protein constituents that act as carriers and pores for active transport across the membrane and facilitated diffusion.
92
Q

what does each amino acid contain? (atoms)

A

C,H,O,N and sometimes Sulfur

93
Q

how many amino acids are proteinogenic and what does that mean

A

only 20
proteinogenic=means that they are found in proteins

94
Q

what does each protein chain of amino acids contain

A

an amino group (-NH2) at one end and a carboxyl group (-COOH) at the other end.

95
Q

what are the three groups that amino acids contain?

A

amino group, R group, carboxyl group

96
Q

what do almost all amino acids end in

A

the -ine group

97
Q

why are some amino acids hydrophobic and some hydrophilic?

A

the R group can vary by size, charge and polarity

98
Q

what happens when amino acids are dissolved in water (key= amino acids act as buffers)

A

when dissolved, the amino group and carboxyl group can dissolve in water- the amino group accepts H= ions (NH2 to NH3+)
the carboxyl group gives up H+ ion so goes from COOH to COO-

99
Q

what are amino acids joined together by

A

by covalent bonds called peptide bonds

100
Q

just like the glyosidic bond and the ester bond, what does making a peptide bond involve

A

a condensation reaction ( breaking= hydrolysis)

101
Q

give an example of peptide bonds being broken (hydrolysed)

A

protease enzymes in the intestine breaking down peptide bonds during digestion.

102
Q

what are two amino acids joined together called?

A

a dipeptide

103
Q

what is it known as when longer chains of amino acids are joined together

A

a polypeptide

104
Q

in terms of chains, what might a protein consist of

A

a single polypeptide chain or more than 1 chain bonded together

105
Q

what’s a primary structure protein

A

sequence of amino acids found in a molecule- sequence of amino acids in a protein chain

106
Q

what’s the secondary structure protein held by (a-helix)

A

the helix is held by hydrogen bonds between the -NH group of one amino acid and the -CO group of another for places ahead of it in the chain.

107
Q

secondary structure, what produces a B-pleated sheet

A

when such chain (zig-zag structure) folds over itself- the hydrogen bonds between the -NH group of one amino acid and the -CO further down the strand hold the sheet together

108
Q

what is quaternary structure?~~

A

many proteins are made up of more than one polypeptide chain (held by same types of bonds that hold tertiary structure)

109
Q

what is the secondary structure primarily held by

A

hydrogen bonds

110
Q

what are the 2 types of proteins

A

fibrous proteins
globular proteins

111
Q

describe fibrous proteins

A

-relatively long, thin structure.
Insoluble in water & metabolically inactive, often has a structure within an organism

112
Q

describe globular proteins

A
  • has molecules of a relatively spherical shape. soluble in water. Often have metabolic roles within the organism
113
Q

what’s a prosthetic group

A

a non-protein component that forms a permanent part of a functioning protein molecule

114
Q

what is the monomer of carbohydrates

A

monosaccharides

115
Q

whats the monomer of proteins

A

amino acids

116
Q

whats the monomer of nucleic acids

A

nucleotides

117
Q

Why is water polar

A

oxygen pulls the electrons towards it making it slightly negative, this makes H slightly positive

118
Q

what is cohesion

A

two or more water molecules attracting each other via hydrogen bonds

119
Q

what is surface tension

A

makes a body of water appear as if there is a film on top. layer able to resist force applied so small animals can walk on it.

120
Q

what will dissolve in water

A

ions and polar molecules

121
Q

is ice less dense than water

A

yes due to structure

122
Q

talk about waters latent heat of vaporisation

A

high latent heat of vaporisation- lots of energy needed to break hydrogen bonds

123
Q

Is water a good solvent

A

good solvent as water is polar

124
Q

2 roles of cholesterol in living organisms

A
  1. regulates fluidity of phospholipid bilayer
  2. converted to steroid
125
Q

what are peptide bonds between(specific)

A

between an amine group and a carboxyl group of another

126
Q

what are the 3 roles of proteins

A
  1. structural role (muscle/tendon)
    2.metabolic role (enzymes)
  2. transport roles (haemoglobin)
127
Q

what can R groups vary in

A

size, polarity, charge
-hydrophobic or hydrophilic properties

128
Q

when is a protein formed

A

when one or many polypeptide chains fold into a specific shape that allows it to form a specific function

129
Q

!what is the secondary structure!

A

the curling or folding of the polypeptide chain into a-helix or b-pleated sheet due to formation of hydrogen bonds

130
Q

what are the 3 bonds formed in tertiary structures

A

-hydrogen bonds (form between polar R groups)
-ionic bonds (formed between positively and negatively charged R groups)
-disulphide bridge (form between sulphur atoms in R groups)

131
Q

!what is the tertiary structure of a protein!

A

the overall specific 3D shape of a protein. This is determined by interactions between R groups and properties of R groups.

132
Q

!what is the quaternary structure of a protein!

A

the specific 3D shape of a protein that is determined by the multiple polypeptide chains and/or the prosthetic group bonded together.

133
Q

what are the 3 globular proteins and their role

A

-haemoglobin- transport protein
-insulin-hormones
-pepsin-enzymes

134
Q

state stuff about haemoglobin

A

-4 polypeptide chains (x2 a-globin x2 b-globin)
- conjugated protein, has a prosthetic group on each polypeptide chain .
transports o2 (4 molecules)

135
Q

state stuff about insulin

A

-a hormone
- maintains blood glucose conc.
soluble in water (hydrophilic R group outside)
- 2 polypeptide chains- one a helix one b pleated- joined by disulphide links

136
Q

state stuff about pepsin

A
  • catalyses digestion of proteins
    -tertiary structure- kept stable by disulphide bonds and hydrogen bonds
137
Q

what are the 3 fibrous proteins and their function

A

collagen- forms tendons
keratin- hardens features eg fingernails
elastin-makes tissues stretchy

138
Q

what is a fibrous protein

A

very long, strong protein- insoluble, structural role

139
Q

state stuff about collagen

A
  • provides strength
    -found in artery walls to prevent vessels from bursting
    -makes tendons allowing skeletons to move
    -used to make bone
    -has crosslinks- chains can form H bonds with adjacent chains
140
Q

state stuff about keratin

A

-hard and strong
-fingernails, horns, hooves
- contains high amount of cysteine- results in disulphide bonds between polypeptide chains

141
Q

state stuff about elastin

A

-can stretch and recoil
- cross linking keep molecules together
-fund in lungs- inflate and deflate
- found in bladder
- found in blood vessel walls

142
Q

3 examples where hydrogen bonds are present in biological molecules??

A

-cellulose
-tertiary structure protein
-quaternary structure protein

143
Q

Describe how the concentration of a reducing sugar can be measured using a colorimeter ?

A

using , standard / known , concentrations (of reducing sugar) ;
heat with , Benedicts (solution) / CuSO4 + NaOH ;
(use of) same volumes of solutions (each time) ;
(use of) excess Benedicts ;
changes to , green / yellow / orange / brown / (brick) red ;
remove precipitate / obtain filtrate ;
calibrate / zero , colorimeter ;
using , a blank / water / unreacted Benedicts ;
use (red) filter ;
reading of , transmission / absorbance ;
more transmission / less absorbance , of filtrate
= more sugar present ; ora
(obtain) calibration curve ;
plotting , transmission / absorbance ,
against (reducing) sugar concentration

144
Q

state and explain ways in which the glucose molecule is well suited to its function in living organisms

A

-soluble so can be transported easily around the organism
-small so can diffuse across membranes
-easily broken down and converted into atp
-molecules can join to form disaccharides or polysaccharides