chapter 1 Flashcards

1
Q

what is a monomer

A

a smaller unit from which larger molecules are made

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

compare structures of cellulose and glycogen

A

-cellulose is made up of B-glucose / glycogen is made up of A-glucose
-cellulose molecule has straight chains / glycogen is branched and coiled
-glycogen has 1-4 / 1-6 glyosidic bonds and cellulose has only 1-4 glyosidic bonds

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

how are starch molecules adapted to their function

A

-insoluble - don’t affect water potential
-helical - compact more in the same space
-large molecules- cannot leave the cell

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

how are cellulose molecules adapted for their function

A

-long and straight chains
-becomes linked together by many hydrogen bonds to form fibrils
-provide strength (to cell wall)

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

how glycogen act as a source of energy

A

hydrolyzed to glucose, glucose is used in respiration

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

features of starch that make it good storage molecule

A

-insoluble in water, don’t change water potential
- branched, molecule is compact
-polymer of A-glucose so provides glucose for respiration
-branched faster enzyme action
- large molecules so it can’t cross the cell membrane

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

test for lipids

A

EMULSION TEST
- add ethanol
-add distill water
-add sample
white emulsion formed

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

test for proteins

A

-add biuret reagent in the sample
- solution changes from blue to purple

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

polymer

A

made from lots of monomers bonded together

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

3 monomers example

A

-glucose
-amino acid
-nucleotide

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

condensation reaction

A

joining two molecules together by removing water

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

hydrolysis reaction

A

slitting apart molecules through addition of water

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

monosaccharide

A

monomers of carbohydrates

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

how are disaccharides formed

A
  • made from 2 monosaccharides
  • joined together by glyosidic bond
  • formed via condensation reaction
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

word equation for formation of disaccharide

A
  • glucose + glucose —-> maltose +water
  • .glucose + fructose —–> sucrose + water
  • glucose + galactose ——> lactose + water
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

test for reducing sugar

A
  • add benedict’s reagent and heat
  • solution turns from blue to orange/ brick red
17
Q

test for non-reducing sugar

A

-following a negative benedict’s test
- add acid and boil ( acid hydrolysis - hydrolysis glyosidic bond
- cool solution then add alkali to neutralize
- add benedicts reagent and heat
- solutions turn from blue to green-red

18
Q

test for starch

A

-add iodine
- solution turns from orange to blue/black

19
Q

triglycerides

A

1 glycerol bonded to 3 fatty acids, they are held by an ester bond

20
Q

saturated fatty acid

A

hydrocarbon chains has only single bonds between carbons

21
Q

unsaturated fatty acid

A

hydrocarbon chains consists of at least one double bond between carbons

22
Q

phospholipids

A

has 2 fatty acids chains a glycerol and a phosphate group

23
Q

reaction that joins amino acids together

A

condensation reaction, peptide bonds form between OH of carboxyl group and a H from an amine group of another amino acid

24
Q

primary structure of protein

A

the sequence of amino acids in a polypeptide chain

25
secondary structure
amino acid sequence coil into alpha helix or beta pleated sheets
26
tertiary structure
further folding of the secondary structure forms a unique 3D shape held in place by ionic hydrogen and disulfide bonds
27
quaternary structure
there's more than 1 polypeptide chain in the protein
28
induced-fit model
the enzyme's active site and substrate are not perfectly complementary in shape initially the enzyme's active site in induced or slightly changes shape, to molded around the substrate, once the substrate binds to the active site
29
enzymes
the active site is unique in shape due to the specific folding and bonding in the tertiary structure of the protein. Due to this specific active site, enzyme can only attach to substrate that are complementary in shape. The enzyme and substrate then form an enzyme-substrate complex
30
factors that effect the rate of enzyme-controlled reactions
- temperature - pH - substrate concentration - Enzyme concentration - inhibitors
31
how does temperature affects the rate of enzyme reactions
at lower temperatures as the temperature increases so does the rate of reaction beyond the optimum temperature the rate of reaction rapidly decreases
32
affect of pH on enzyme action
low pH: there will be an excess of H+ ions, this can break the ionic and hydrogen bonds holding tertiary structure causes active site to change shape high pH: there will be an excess of OH- ions released which can break hydrogen and ionic bonds changes shape of active site
33
how does enzyme concentration affects enzyme reaction
at a low concentration enzyme concentration is the limiting factor when more enzyme is added rate increases more available active site more successful collisions
34
how substrate concentration effects enzyme reactions
at low concentration substrate is limiting factor more substrate is added the rate increases there will be more successful collisions
35
competitive inhibitors
same shape as the substrate and can bind to the active site prevents the substrate t bind no enzyme-substrate complex formed no reaction can happen
36
non-competitive inhibitor
binds to the enzyme away from the active site in the allosteric site causes the active site to change shape substrate can't bind to substrate