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Biology A level > Enzymes and Proteins > Flashcards

Enzymes and Proteins Flashcards

Module 1

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1
Q

What is the general structure of an amino acid

A

Amino group, carboxylic acid group and R group

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2
Q

How many different amino acids are there

A

20

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3
Q

How are two amino acids bonded together and what molecule does this produce

A

By peptide bonds, produces a dipeptide
condensation reaction

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4
Q

How long is a peptide chain

A

Any length

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5
Q

What is the primary structure of a protein

A

Polypeptide chain held together by peptide bonds

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6
Q

What is the secondary structure of a protein

A

Areas of initial folding
- Alpha Helices or Beta pleated sheets
held together by hydrogen bonds

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7
Q

What is the tertiary structure in proteins

A

Interactions of R group
3D shape
4 types of bond:
- Hydrogen bonds
- Ionic Bonds
- Disulphide bridge
- Hydrophobic interactions

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8
Q

What are Disulphide bridges

A

Cysteine contains sulphur, when 2 cysteines are close, double covalent bonds form
V. strong

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9
Q

What is the Quaternary structure of an enzyme

A

2+ polypeptides join together
Or there is a prosthetic group

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10
Q

What is a conjugated protein

A

A globular protein with a prosthetic group

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11
Q

What happens to Fibrous and globular proteins when they denature

A

Fibrous - lose structural strength
Globular - insoluble and inactive

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12
Q

What are Fibrous proteins

A

Long rope like fibres with high tensile strength and are generally insoluble in water
eg:
- collagen, Keratin, Elastin

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13
Q

What does Collagen do?

A

Main component of connective tissue like ligaments, tendons, cartilage

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14
Q

What does keratin do

A

main component of hard structures like hair, nails, claws, feathers and hooves

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15
Q

What does Elastin do

A

Major protein component of tissues that require elasticity like arteries, lungs, skin, etc.

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16
Q

What are globular proteins

A

They have a spherical shape caused by tightly folded polypeptide chains, hydrophobic groups in, hydrophilic out - makes it soluble in water
- transport proteins, enzymes, hormones

17
Q

What are the features of Haemoglobin

A

globular protein, 4 polypeptide chain subunit *2 alpha, 2 beta)
4 haem/prosthetic groups contain Fe2+ within 4 subunits
Conjugated protein
Soluble

18
Q

Feature of amylase

A

Globular protein
Soluble
single chain of amino acids
secondary has alpha helices and beta pleated sheets
only works if a co-factor Cl- is bound to it

19
Q

Insulin properties

A

Globular protein
soluble
two amino acids joined by disulphide bonds

20
Q

What happens when an enzyme is placed in the wrong pH

A

active site denatures because the different number of H+ ions cause reaction which alter the tertiary structure of the enzyme. This means the substrate is no longer complimentary to the active site of the enzymes

21
Q

What are the different types of inhibitors

A

Competitive
Non competitive
Permanent

22
Q

What are competitive inhibitors

A

Similar shape to substrate, occupy active site temporarily to form enzyme-inhibitor complex
substrate cannot fit so no reaction is catalysed

23
Q

What are non competitive inhibitors?

A

Attach to allosteric site, distorts 3D tertiary structure which changes enzymes active site. Substrate can no longer fit into active site

24
Q

What are permanent inhibitors

A

Irreversible as it denatures enzyme

25
Q

What is a cofactor

A

Non-protein substance needed before enzymes can catalyse a reaction

26
Q

What are prosthetic group cofactors

A

form permanent part of enzymes

27
Q

What are inorganic ion cofactors

A

Ions that increase rate of reaction
can combine with enzyme or substrate so that enzyme-substrate complex can fomr easier by changing distribution and sometimes shape

28
Q

What are coenzymes

A

small organic and non protein
temporarily bind to active site
can be reused
carry chemical groups between enzymes

29
Q

Why are things poisonous

A

because they inhibit or over activate enzymes

29
Q

Example of extracellular and intracellular enzym

A

intra: DNA polymerase
extra: lipase

29
Q

What is product inhibition

A

When the product inhibits one of the first enzyme in a metabolic pathway in order to control the reaction

30
Q

What happens if the temperature is too high for an exyme

A

More KE means more vibrations
This breaks H and ionic bonds, changing active site shape
tertiary unravels
enzyme denatures

31
Q

Draw the general structure of a Amino Acid

A

Has R group, amine group and carboxylic acid group

Biology A level (19 decks)

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