Brainscape's Knowledge GenomeTM

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


See full index

Bio 2 back up > unit 1 > Flashcards

unit 1 Flashcards

You may prefer our related Brainscape-certified flashcards:
Biology 101 flashcards
1
Q

Describe the difference between matter and element

A

matter= anything that takes up space and has mass
element=building blocks of matter

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

Whats the difference between a molecule and compound

A

molecule= atoms of same element
compound= atoms of different elements

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

What are the most abundant elements in our bodies

A

Nitrogen, carbon, oxygen, calcium and hydrogen

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

How do isotopes differ from eachother

A

they have different number of neutrons

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

What is the relationship between electrons and chemical bonds

A

chemical bonds happen because of valence e- who want to achieve an octet

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

Which bonds are formed between molecules

A

H-bonds, covalent and ionic

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

which bonds are formed between atoms

A

ionic/(polar and non-polar)covalent bonds

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

what are the 2 types of strong bonds and how do they differ

A

covalent (sharing e-) and ionic (complete transfer of e-)

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

What is the relationship between covalent bonds, electronegativity, polar and nonpolar
compounds?

A

polarity depends on difference in electronegativity between atoms
Polar bonds happen when atoms do not share electrons equally
Non-polar bonds share e- equally

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

Of the most abundant elements in your body, what is the relative electronegative to each other?

A

Ca

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

What are examples of non-polar molecules and polar molecules?

A

non-polar= CH4
polar= H2O

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

what are the 3 types of weak bonds

A

1-H-bonds
2-Van der Waals interactions
3-Ionic bonds in water

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

whats the purpose of weak bonds

A

they allow molecules to interact, provide stability in large molecules,
adhering molecules briefly when they collide

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

why do ionic bonds weaken in water

A

each ion is partially shielded because it interacts with water (they dissociate easily in water)

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

in photosynthesis where does oxygen come from

A

water and CO2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Why do all organism need water

A

the main source of oxygen (medium of life)

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

why is water polar

A

the slight positive charges on the hydrogens and the negative charges of oxygen create partial charge/dipole moment making the molecule polar

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

Define cohesion

A

the ability of molecules of same substance to stick together

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

define adhesion

A

the ability of molecules to stick to another material

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

define tension

A

mesures how difficutl it is to break/stretch surface of a liquid

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

what are the four main properties of water

A

1-solvent
2-C.A.T
3-temperature buffer
4-Density

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

Why is water a universal solvent

A

can dissolve any polar substance

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

what is hydration

A

solvation for which the solvent is water

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

True of false
water can dissolve non polar substances

A

false

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

how does water dissolve ionic substances

A

in ionic solid, the partial + charge of hydrogens attract the anion an - charge of oxygen attract cation= they separate and solid is dissolved

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

How can water dissolve non polar substances like sugar

A

Water forms H-bonds with outer molecules and removes the monosaccharides individually until they are dispersed throughout the solution

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

What other kind of macromolecules can dissolve in water

A

proteins if they have ionic areas

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

where can water be found as a solvent in organisms

A

in the blood, inside cell (cytosol), plant sap

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

What cause cohesion between water molecules

A

H-bonding

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

Why is cohesion and adhesion useful for organisms

A

allows for capillary action

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

Define capillary action

A

tendency of water to move in narrow tubes, against gravity (ex: water moves from root to leaves)

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

why does water have a strong surfcae tension

A

strong attraction between molecules (H-bonds)

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

wnat is the max amount of H-bonds that a molecule can form

A

4

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

How does each state of water vary in terms of H-bonds

A

in solid water each molecules have 4 H-bonds, liquid have less and air have practically none.

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

Why is it important for water to have a high specific heat

A

allows water to absorb large amount of heat before its temperature increases

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

How does water act like a temperature buffer

A

high specific heat= better ability to resist temperature change

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

Why is moderation of temperature important to maintain life

A

allows oceans, lakes, etc to maintain relatively constant temperature= stable environment

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

What is evaporative cooling

A

when water is heated , the molecules that are released fatser enter gas phase and the water left behind is more cool

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

how do organisms utilize evaporative cooling

A

to help cool themselves (perspire/transpires)

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

What are the properties of ice

A

contains more stable hydrogen bonds
Ice is less dense than liquid water

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

Why is it important that ice is less dense than water

A

if ice sank it woud freeze the bottom of the oceans=life unsustainable

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

what is ionization

A

water molecules can break apart in aqueous solutions (H+ and OH-

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

What is the effect of a acid on pH of solution

A

decreases pH (donates H+)

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

What is the effect of a base on pH of solution

A

increases pH (donate OH-

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

Describe a pH buffer

A

substance that resists changes in pH by either accepting H+ ions in excess and donate H+ when they’re missing

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

Name a buffer

A

blood

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

Why is it important for pH in cells and in other body fluids to be tightly regulated?

A

any pH change could disrupt ionic/h-bonds between amino acids structure = unstable protein
can alter protein shape= cant function

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

How does carbonic acid (H2CO3) play a role in the fluids of the body?

A

acts as buffer in human blood to keep it within range

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

what can cause blood pH to go below range

A

respiratory disease= the body can get rid of CO2 fast again= increase H+ concentration= acidosis

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

what can cause blood pH to go above range

A

hyperventilation= too much CO2 expelled= decrease in H+= alkalosis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

Why do shells in aquatic animals thin and become fragile as oceans become more and more acidic?

A

they require calcium carbonate to make their shells and increase in H+ disturbed and it causes this rxn :H+ + CO32- =HCO3- which decreases calcium carbonate production

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

Where do autotrophs obtain organic carbon? Heterotrophs?

A

autotrophs obtain their carbon from light or chemical energy (atospheric CO2)
heterotrophs obtain their carbon from organic compounds

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

what is an biomolecule

A

proteins, DNA, carbohydrates and lipids

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

whats an organic molecule in biology

A

compounds formed by the living that contain a carbon hydrogen backbone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

Whats a carbon skeleton

A

carbons of organic compounds

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

whats a functional group

A

elements that are attached to the carbon skeleton (noncarbon grps)

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

Which properties of carbon make it a good building block for organic biomolecules?

A

Has a tetravalence which makes large/complex molecules possible.

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

Which other elements make up the major atoms used to build biomolecules?

A

hydrogen, nitrogen, oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

When carbon is bound to four other atoms, what shape does the molecule generally take?

A

tetrahedral shape

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

what is polarity

A

the measure of electronegativity between two atoms (how much they can pull e- )

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

List the seven functional groups discussed

A

hydroxyl grp
carbonyl grp
carboxyl grp
amino grp
sulfhydryl grp
phosphate grp
methyl grp

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

what are the general properties of the hydroxyl grp

A

OH-
polar grp, doesnt dissociate in water

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

what are the general properties of the carbonyl grp

A

CO-
provide some degree of polarity.

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

what are the two types of carbonyl groups

A

aldehydes and ketones

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

whats the difference between aldehyde and a ketone

A

aldehydes contain the carbonyl carbon bonded to AT LEAST one H
ketones have carbonyl carbon bonded to 2 other carbons

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

True or false
simple sugars can only be aldehydes

A

false can also be ketones

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

What structures do monosaccharides take on when mixed with a fluid (i.e. water)

A

ring structure

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

what are the general properties of the carboxyl grp

A

-COOH
weakly acidic (can release proton)
provides polarity

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

Carboxyl group is an important part of what macromolecule (monomer)

A

amino acids (in protein)

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

what are the general properties of the amino grp

A

-NH2
polar, allows amino acids to act as organic buffers (can be acid or base ), weakly basic

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

In amino acids does the amino group accept or donate a proton

A

accepts a proton

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

why can amino acids act as natural buffers

A

they have a carboxyl grp (acid) and an amino grp (basic) in their structure.

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

what are the general properties of the sulfhydryl grp

A

-SH
non polar, forms disulfide bridges

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

what are the general properties of the phosphate grp

A

-OPO3 2-
polar, can donate H+ into solution= weakly acidic

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

Why are disulfide bridges important

A

strong bonds that help stabilize the internal structure of proteins (form cross links)

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

In what important molecules can phosphate groups be found

A

in phospholipids, nucleotides and ATP

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

Why is atp so high in energy

A

the 3 phosphate grp bonded to eachother are highly unstable (repulse one another)= high E bonds

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

what are the general properties of the methyl grp

A

-CH3
nonpolar, acts as an identity tag to molecules (read by enzymes)

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

Where can sulfhydryl groups be found

A

in proteins (internal structure)

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

Where can amino groups be found

A

amino acids, nitrogenous bases of DNA/RNA

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

how does the carbonskeleton contribute to the diversity of organic biomolecules

A

the arragement of the carbon skeleton gives them different properties

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

how do the functional groups contribute to the diversity of organic biomolecules

A

they can give them unique properties/behaviors

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

define isomers

A

compounds with the same molecular formula but different chemical structures=diff properties

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

what are the 3 kinds of isomers

A

structural-geometric-optical

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

Whats the difference between a structural and geometrical isomer

A

structural: different covalent arrangement of their atoms

geometric: same covalent arrangement but different spatial arrangement

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

what are the 2 types of geometric isomers

A

cis and trans isomers

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

How do cis isomers differ from trans isomers

A

cis= groups on same side

trans= grps on opposite sides of the bond

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

give an example of a geometric isomer

A

rhodopsin

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

what are enantiomers

A

isomers that are the images of each other (cant be superimposed)

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

True or false
Cell will only recognize one enantiomer

A

true

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

Why is it important to be aware of enantiomers

A

give different effect to drugs (ex: thalidomide)

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

Define a monomer and a polymer

A

monomer: small organic molecule that are joined to make larger molecule=macromolecules

polymers: thousands of monomers covalently joined together.

93
Q

Describe a hydrolysis reaction

A

breaks down polymers into monomers by adding water to break the bonds

94
Q

Describe a condensation/ dehydration reaction

A

removing H/OH- grps to link monomers and form polymers
requires energy and a catalyst

95
Q

Why do hydrolysis and condensation reactions require enzymes

A

to speed up the reactions

96
Q

What are the major functions of carbohydrates in cells. (Give some specific examples for each)

A

short term energy storage (sugar) and intermediate energy storage (glycogen and starch)
structural components in cells (chitin and cellulose)

97
Q

What is the general ratio of the three main atoms in a carbohydrate?

A

1:2:1

98
Q

Fill in the blank :

Carbohydrate are ____ and ____ compounds with multiple -OH grps

A

aldehyde and ketone

99
Q

what are the common disaccharides found in our bodies

A

sucrose, maltose and lactose

100
Q

What are three monosaccharides that mammals can metabolize? How do they differ from each
other?

A

glucose, fructose and galactose
they all have different structures but the same chemical formula (structural isomers)

101
Q

whats the most common monosaccharide

A

glucose

102
Q

List the structural characteristics of a monosaccharide that can vary

A

spatial arrangement of the carbon skeleton, the position of carbonyl grp, size of skeleton

103
Q

Define aldose

A

the carbonyl group is at the end

104
Q

define ketose

A

the carbonyl grp is in the middle

105
Q

Whats a triose sugar

A

has 3 carbon, smallest sugar

106
Q

whats the difference between a pentose and hexose sugar

A

pentose=5 carbon
hexose= 6 carbon

107
Q

where can pentose sugars be found

A

in DNA

108
Q

Why do monosaccharides have isomers

A

They occur naturally in the wild and they also provide polysaccharides with different properties

109
Q

What is glycosidic linkage

A

covalent bond that links monosaccharide together after dehydration synthesis run

110
Q

what are the two kinds of glycosidic linkage

A

alpha and beta

111
Q

what are the 2 isomeric forms in which glucose exists

A

β-glucose and α-glucose

112
Q

glucose is the end product of what reaction

A

photosynthesis

113
Q

glucose is a reactant in which rxn

A

cellular respiration

114
Q

How does your body maintain homeostasis of glucose in your blood?

A

The pancreas secretes hormones (insulin and glucagon) that regulates the bloog sugar levels

115
Q

Which organs and tissues are involved in maintaining blood glucose level constant

A

liver and pancreas

116
Q

What is the function of insulin

A

it decreases blood glucose level by :
1. stimulating uptake of glucose in muscle
2. preventing breakdown of glycogen → glucose in the liver
3. stimulates adipose cell to store glucose as fat

117
Q

How does insulin function

A

the hormone binds to receptors on surface of fat, mucle and liver cells and promotes the uptake of glucose inside the cell

118
Q

What is the function of glucagon

A

it increase the glucose level in the blood by:
1.Stimulating conversion of glycogen→ glucose
2. breaks down proteins into amino acids (muscle cells)
3. breaks down fats in adipose cell to release fatty acids

119
Q

how does breakdown proteins release blood glucose

A

amino acids are involved in gluconeogenesis (synthesis of glucose )

120
Q

What kind of disorder is diabetes mellitus

A

endocrine disorder (hormonal isssue)

121
Q

What cause diabetes

A

deficiency of insulin (type 1)
decreased reponse to insulin (type 2)

122
Q

What are the symptoms of diabetes

A

excess pee, low energy, dehydration, hunger, etc…

123
Q

Why are disaccharides and starch important in our bodies

A

they are the main source of glucose in food

124
Q

Which monosaccharides are involved in the following disaccharides: maltose,
sucrose, lactose.

A

Maltose: glucose +glucose
Sucrose: fructose +glucose
Lactose : galactose+ glucose

125
Q

what is lactose intolerance

A

drop in lactase production

126
Q

What is lactase and why is it important

A

enzyme that breaks down lactose in our small intestine

127
Q

In what organ are carbohydrates usually absorbed as monosaccharides

A

the small intestine

128
Q

What does lactorance intolerance cause

A

the lack of lactase in small intestine cause lactose to pass in the large intestine and gets broken down by bacteria= causes gases and acids

129
Q

What is the treatment for lactose intolerance

A

removing lactose from the diet

130
Q

What are oligosaccharides

A

small sugars (2-6 units) that are attached to glycoproteins and some glycolipids

131
Q

What is the function of oligosaccharides

A

serves as tags to identify cells (heart, muscle cell, etc)

132
Q

What is the cause of flatulence from eating legumes?

A

particular oligosaccharides present in beans/legumes that our body can digest (no enzymes for it)

133
Q

What is the role of glycoproteins

A

serve in cell adherence, protection and identification

134
Q

Where are glycoproteins found generally

A

in the ECM
also found in mucus

135
Q

why do polysaccharides vary in their properties

A

composed of different isomers and have different structures (branched, webbed, etc)

136
Q

Describe the two functional classes of polysaccharides.

A

Energy storage : molecules that can easily be broken down
Structural: molecules with specific 3-D arrangements

137
Q

What are the characteristics of α-linkages

A

present in sugars/starch that allows molecules to be broken down and used as energy source

138
Q

What are the characteristics of β-linkages

A

occurs in structural molecules and cant be digested by most eukaryotes

139
Q

Why is glycogen is an efficient storage molecule

A

can be broken down into glucose-6-phosphate which give short term energy for metabolism

140
Q

What is starch hydrolized into and what enzyme is responsible for that

A

amylase hydrolizes starch into maltose

141
Q

where can amylase be found

A

saliva and secreted by pancreas

142
Q

What makes the structure of cellulose great for fibers

A

extensive unbranched chain of β-glucose which allows for H-bonds inbetween cellulose molecules

143
Q

What is dietary fiber?

A

carbs needed for proeper digestion (ex: cellulose) but we lack the enzyes to hydrolize them into monosaccharides (NOT USED FOR ENERGY)

144
Q

Describe the importance of dietary fiber in our diet

A

fiber adds bulk and absorbs water= makes feces larger and softer:
-reduces pressure for defecation
-can lower cholesterol
-slows rate of carb absorption

145
Q

Describe the structure of chitin

A

unbranched polysaccharide

146
Q

Whats the only polysaccharide with an amino acid attached to it

A

chitin

147
Q

What is the function of chitin

A

protective exoskeleton of arthropods
ccan also be used for surgical threads

148
Q

Where is peptidoglycan found

A

in cell walls of bacteria

149
Q

What is the difference between gram positive and gram negative bacteria

A

gram (+): cell wall with a lot of peptidoglycan
gram (-): cell wall lacking peptidoglycan

150
Q

why is gram staining a valuable too in medicine

A

allows us to identify why antibiotic will be efficient to treat an infection
ex: penicillin kills gram positive bacteria

151
Q

what is the difference in bonding between structural and energy storage polysaccharides

A

structural: β-linkages
energy: α-linkages

152
Q

Why are lipids grouped together

A

they’re all hydrophobic molecules

153
Q

What are the classes of lipids

A

neutral fats (fatty acids and triglycerides), phospholipids and steroids,

154
Q

true or false
Triglycerides are neutral fats

A

true

155
Q

What is the function of neutral fats in organism

A

serve in energy storage, insulation of organs

156
Q

What is the structure of triglycerides

A

1 glycerol and 3 fatty acids (long hydrocarbon tail with carboxyl grp)

157
Q

How many reactions does it take to make one triglyceride

A

3 dehydration reactions

158
Q

What bonds join glycerol with 3 fatty acids

A

ester linkages

159
Q

What allows tryglycerides to have different properties

A

the fatty acids chain

160
Q

what are the 3 kinds fatty acids

A

1-saturated fatty acids: no double bonds in the hydrocarbon tail
2- monunsaturated: 1 double bond
3-polyunsaturated: 2 or more double bonds

161
Q

Fill in the blank:
saturated fatty acids have a ____ structure while mono/polyunsaturated fatty acids have a ______ structure

A

linear and bent

162
Q

how do the structure of fatty acids affect their state at room temperature?

A

bent= molecules cant stack well=liquid at room temperature
linear=molecules can stack= solid at room temp

163
Q

What kind of fatty acid can come in the cis or trans shape

A

unsaturated

164
Q

what is the general structure of a cis unsaturated fatty acid (orientation of the bond)

A

both H are on the same side of the double bond (creates the bend)

165
Q

what is the general structure of a trans unsaturated fatty acid (orientation of the bond)

A

Hydrogens are on opposite side of double bond (creates amore rigid/linear structure)

166
Q

Which kind of unsaturated are found naturally and which are processed food (cis or trans)

A

natural:cis
processed: trans

167
Q

why are trans fat bad for our health

A

overconsumption of trans fat can lead to blockages in our arteries (since they’re dense and solid)

168
Q

how are trans fats synthesized

A

through hydrogenation

169
Q

Describe hydrogenation

A

H atoms are added to cis unsaturated fatty acids= makes fat more solid at room temp this converts cis bonds→ trans bonds or make fat unsaturated

170
Q

Describe briefly how triglycerides are digested

A

fats are emulsified by bile salts (made by the liver). They are then hydrolized into fatty acids and absorbed by cells in lining of small intestine

171
Q

What happens to fatty acids onced they’re absorbed by the small intestine

A

they are reassembled into chylomicrons

172
Q

What’s the function of chylomicrons

A

lipoproteins that carry lipids in the blood/to other cells in the body

173
Q

describe the general structure of lipoproteins

A

spherical molecules with hydrophobic interior and hydrophilic exterior
embedded with proteins

174
Q

What are LDLs

A

low-density liproteins that carry fats produced by the liver to other cells

175
Q

what are HDLs

A

high-density lipoproteins that return to the liver after delivering fatt cells to the body

176
Q

what differentiates HDL from LDL from chylomicrons

A

HDL are mostly proteins
LDL are mostly fat
Both LDL and HDL are involded with the liver while chylomicrons are made in small intestine
LDL/HDL are the remaining chylomicrons with the excess fats

177
Q

What is the structure of steroids

A

4 fused carbon rings with various functional grps attached

178
Q

Give examples of steroids

A

cholesterol, testosterone, vitamins, bile salts, etc

179
Q

what are annabolic steroids

A

synthesized steroids similar to testosterone that promotes muscle growth

180
Q

How is cholesterol carried through the blood

A

through LDLs/HDLs

181
Q

How can we determine if someone has good or bad cholesterol

A

by mesuring HDL, LDL levels in the blood

182
Q

what does it mean when someone has “bad” cholesterol

A

high levels of LDLs in the blood because of high trans fat diet= can cause plaque in blood vessels

183
Q

what does it mean when someone has “good” cholesterol

A

high levels of HDLs circulating in the blood to reduce presence of cholesterol in the blood

184
Q

Describe the structure of phospholipids

A

glycerol, 2 fatty acids, phosphate grp (- charge) and an alcohol (choline)

185
Q

What special traits do phospholipids have

A

theyre amphipatic

186
Q

What is the main function of phospholipids

A

make up all cell membrane

187
Q

what are the 2 types of phospholipids that can be found in cell membrane

A

phosphoglyceride and shingolipids

188
Q

what makes shingolipids different

A

they have a single leg and have amino alcohol instead of glycerol

189
Q

in what cells are shingolipids more abundant

A

neurons, spin cells, lungs

190
Q

What happens to sphingolipids in patients with Tay-Sachs disease?

A

accumulation of shingolipids in nerve cells which leads to the destruction of nervous system

191
Q

which group is responsible for the specific properties of an amino acid

A

The side chain (R)

192
Q

What do we call the bond that links amino acids to make a polypeptide

A

peptide bonds

193
Q

What are α, β and γ forms of amino acids?

A

α: α carbon is bonded to the carboxyl and amino grp
β: β carbon is linked to amino acid and α carbon is linked to carboxyl grp
γ: GABA amino acid (3 carbons)

194
Q

true of false
the gamma form of amino acids is the most common

A

false
alpha form is the most common

195
Q

Fill in the blank
L and D isomers of amino acids are ______.

A

enantiomers

196
Q

Which isomers of amino acids are used as building blocks for proteins

A

L isomers

197
Q

Why are amino acids great biological buffers

A

depending on the environment they either accept a proton to increase pH (becomes protonated) or donates a proton to lower pH (becomes dissociated)

198
Q

Whats a zwitterion

A

the amino acid present at a dipolar ionic state when pH=7.4 (neutral)

199
Q

What are the 3 classes side chain attached to amino acids

A

polar, electrically charged non polar (neutral)

200
Q

List 4 hydrophobic amino acids

A

leucine, methionine, isoleucine, tryptophan

201
Q

Whats an essential amino acid

A

amino acid that an animal can’t synthesize on their own, so it must come from food

202
Q

Define a polypeptide

A

repeating structure of amino acids linked together

203
Q

what provides polarity to the polypeptide

A

the N-terminus and C-terminus

204
Q

whats the difference between a polypeptide and a protein

A

protein: macromolecule made of one or more polypetide coiled/twisted together

polypeptide: unique amino acid chain

205
Q

Describe the primary structure of a protein

A

unique sequence of amino acids

206
Q

Describe the secondary structure of a protein

A

H-bonds between the amino grps and carboxyl grp (alpha helix or beta pleated sheets)

207
Q

Describe the tertiary structure of a protein

A

3-D shape of the folded protein cause by interaction amongst the R grp (H-bonds, disulfide bridges, ionic bonds, hydrophobic interactions )

208
Q

what are the common types of tertiary structure

A

globular (mix of beta pleated sheets and alpha helix) or fibrous (mostly alpha helix)

209
Q

Describe the quaternary structure of a protein

A

interactions amongst polypetide chains

210
Q

True of false
The protein shape and primary structure defines its function

A

true

211
Q

what is the function of chaperonins

A

complex molecules that ensure a proetin is properly folded and assumes the right conformation

212
Q

Whats a monomeric protein

A

no quaternary structure

213
Q

whats an oligomeric protein

A

two or more polypeptide chains

214
Q

Define denaturation

A

disruption of the secondary and tertiary structure of a protein which destroys its shape=can no longer function

215
Q

Would a change in the amino acid chain be considered as denaturation

A

no , denaturation stems from external factors. an error in amino acid chain can only be cause by a genetic mutation

216
Q

what factors can cause denaturation

A

heat, alcohol, pH imbalance

217
Q

What is a prion

A

a misfolded protein that becomes an infection agent and force other proteins to misfold.

218
Q

How does prion disease occur

A

the disfunctional version of the protein binds to a normal one and causes it to misfold, this new prion then goes on to denature other proteins.

219
Q

what are the 8 functions of proteins

A

1- enzymatic
2-defensive
3-Structural
4-Contractile and motor
5-Transport
6-Receptor
7-Storage
8-Chemical messanger

220
Q

Whats the function of enzymatic protein

A

accelerate chemical rxn
ex: any enzyme

221
Q

whats the function of storage proteins

A

serve as source of amino acids for embryos/infant
ex: casein or ovalbumin

222
Q

whats the function of chemical messenger proteins

A

coordinate an organism’s activity=hormones or neurotransmitters
ex: insuline or ACh

223
Q

whats the function of contractile proteins

A

functions in mouvement
ex: actin and myosin

224
Q

whats the function of defensive proteins

A

protection against diseases
ex: antibody proteins=antigens that help destroy the foreign body

225
Q

whats the function of transport proteins

A

transport substances in the body/cells
ex: hemoglobin

226
Q

whats the function of receptor proteins

A

regulate response of the cell to stimuli
ex: receptors in nerve cells

227
Q

whats the function of structural proteins

A

provide support (in cell membrane, muscle tissue, tendons, ligaments)
ex: collagen, elastin

228
Q

Whats a simple protein

A

only made of amino acids

229
Q

whats a conjugated protein

A

contains amino acids and another chemical grp and a prosthetic grp

Bio 2 back up (2 decks)

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