Ch1 Proteins and Enzymes Flashcards

1
Q

Amino acid groups

A
  1. amine NH2
  2. carboxyl COOH
  3. hydrogen H
  4. R group
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2
Q

Globular protein

A
  1. soluble
  2. specific tertiary structure
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3
Q

Fibrous protein

A
  1. strong
  2. insoluble
  3. inflexible
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4
Q

Primary structure

A
  1. sequence of amino acids
  2. condensation reaction between COOH and NH2
  3. peptide bonds
  4. polypeptide chain
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5
Q

Secondary structure

A
  1. primary structure coils to form helix
  2. held by hydrogen bonds
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6
Q

Tertiary structure

A
  1. secondary structure folds to form specific 3D shape
  2. ionic bonds
  3. hydrogen bonds
  4. disulfide bridges
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7
Q

Quaternary structure

A
  1. multiple polypeptide chains
  2. associated with prosthetic groups
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8
Q

Test for proteins

A
  1. Add biuret reagents (sodium hydroxide then copper (II) sulfate)
  2. blue to purple colour
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9
Q

Structure of collagen

A
  1. made of glycine
  2. forms tight coil with little branching
  3. coiled into secondary helix
  4. 3 tertiary structures wrap around
  5. fibrous protein used in tendons
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10
Q

Enzymes

A
  1. catalysts
  2. speed up rate of reaction by lowering activation energy
  3. recycled
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11
Q

Enzyme structure

A
  1. globular protein
  2. specific active site shape
  3. complementary to substrate
  4. bind to form enzyme- substrate complex
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12
Q

Induced fit model

A
  1. active site changes shape
  2. substrate binds to active site
  3. active site moulds around substrate
  4. forms enzyme-substrate complex
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13
Q

Lock and key theory

A
  1. active site is rigid
  2. only complementary substrate binds
  3. form enzyme-substrate complex
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14
Q

Temperature on enzyme activity

A
  1. kinetic energy increases
  2. molecules move faster
  3. increased chance of successful collisions
  4. increased chance of ES complex
  5. increase rate of reaction
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15
Q

Too high temperature on enzyme activity

A
  1. bonds in tertiary structure break
  2. loses active site shape
  3. substrate no longer complementary
  4. can’t form EX complex
  5. enzyme denatured
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16
Q

pH on enzyme acitvity

A
  1. bonds in tertiary structure break
  2. alters charged on amino acids
  3. loses active site shape
  4. substrate no longer complementary
  5. can’t form EX complex
  6. enzyme denatured
17
Q

Why normal enzyme action plateauxs

A
  1. little amount of substrate
  2. products block
  3. difficult for enzyme substrate molecules to form
18
Q

Affects of increased substrate concentration

A
  1. increased chance of successful collisions
  2. increased chance of forming an ES complex
  3. increased rate of reaction
  4. continues until all enzyme active sites are full
19
Q

Competitive inhibitor

A
  1. similair shape to substrate
  2. complementary shape to active site
  3. blocks active site
  4. prevents ES complexes from forming
20
Q

Non-competitive inhibitor

A
  1. binds to another site on enzyme
  2. enzyme shape changes- alters active site
  3. no ES complexes can form
21
Q

Affect of enzyme concentration

A
  1. it is limiting
  2. if all active sites saturated, rate stays the same
22
Q

Activation energy

A

minimum amount of energy required for reaction to take place