Ch1 Proteins and Enzymes Flashcards
1
Q
Amino acid groups
A
- amine NH2
- carboxyl COOH
- hydrogen H
- R group
2
Q
Globular protein
A
- soluble
- specific tertiary structure
3
Q
Fibrous protein
A
- strong
- insoluble
- inflexible
4
Q
Primary structure
A
- sequence of amino acids
- condensation reaction between COOH and NH2
- peptide bonds
- polypeptide chain
5
Q
Secondary structure
A
- primary structure coils to form helix
- held by hydrogen bonds
6
Q
Tertiary structure
A
- secondary structure folds to form specific 3D shape
- ionic bonds
- hydrogen bonds
- disulfide bridges
7
Q
Quaternary structure
A
- multiple polypeptide chains
- associated with prosthetic groups
8
Q
Test for proteins
A
- Add biuret reagents (sodium hydroxide then copper (II) sulfate)
- blue to purple colour
9
Q
Structure of collagen
A
- made of glycine
- forms tight coil with little branching
- coiled into secondary helix
- 3 tertiary structures wrap around
- fibrous protein used in tendons
10
Q
Enzymes
A
- catalysts
- speed up rate of reaction by lowering activation energy
- recycled
11
Q
Enzyme structure
A
- globular protein
- specific active site shape
- complementary to substrate
- bind to form enzyme- substrate complex
12
Q
Induced fit model
A
- active site changes shape
- substrate binds to active site
- active site moulds around substrate
- forms enzyme-substrate complex
13
Q
Lock and key theory
A
- active site is rigid
- only complementary substrate binds
- form enzyme-substrate complex
14
Q
Temperature on enzyme activity
A
- kinetic energy increases
- molecules move faster
- increased chance of successful collisions
- increased chance of ES complex
- increase rate of reaction
15
Q
Too high temperature on enzyme activity
A
- bonds in tertiary structure break
- loses active site shape
- substrate no longer complementary
- can’t form EX complex
- enzyme denatured
16
Q
pH on enzyme acitvity
A
- bonds in tertiary structure break
- alters charged on amino acids
- loses active site shape
- substrate no longer complementary
- can’t form EX complex
- enzyme denatured
17
Q
Why normal enzyme action plateauxs
A
- little amount of substrate
- products block
- difficult for enzyme substrate molecules to form
18
Q
Affects of increased substrate concentration
A
- increased chance of successful collisions
- increased chance of forming an ES complex
- increased rate of reaction
- continues until all enzyme active sites are full
19
Q
Competitive inhibitor
A
- similair shape to substrate
- complementary shape to active site
- blocks active site
- prevents ES complexes from forming
20
Q
Non-competitive inhibitor
A
- binds to another site on enzyme
- enzyme shape changes- alters active site
- no ES complexes can form
21
Q
Affect of enzyme concentration
A
- it is limiting
- if all active sites saturated, rate stays the same
22
Q
Activation energy
A
minimum amount of energy required for reaction to take place