Proteins and Enzymes Flashcards

1
Q

Bonds to stabilise a chains

A

Hydrogen

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2
Q

Primary structure

A

Sequence of amino acids- held by peptide bonds

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3
Q

Secondary structure

A

a helix or b sheet

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4
Q

Tertiary structure

A

internal hydrophobic, external hydrophilic

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5
Q

Quarternary

A

many polypeptide chains

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6
Q

What forms in the brain of a person with Alzheimers?

A

insoluble amyloid fibrils

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7
Q

Creutzfeldt Jacob disease

A

infectious prion protein -> insoluble aggregate

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8
Q

Myoglobin

A

a helices, O2 store

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9
Q

Haemoglobin

A

2 a and 2 b chains, O2 transporter, lower affinity to O2

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10
Q

Haem

A

tightly bound; with protein will keep Fe in ionic form and inhibit CO binding

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11
Q

T state

A

low affinity for O2- more salt bridges

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12
Q

R state

A

high affinity for O2

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13
Q

Bohr effect

A

increase in H+ decreases Hb O2 affinity -> more salt bridges -> T state

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14
Q

Higher BPG at altidude…

A

low affinity for O2 -> more O2 release

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15
Q

Collagen

A

Gly, Pro and Hyp alpha helix (gly in centre) Form staggered microfibrils (type I, II and III) with cross links

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16
Q

Collagenases..

A

break down collagen

17
Q

Ehlers-Danlos

A

stretchy skin and loose joints

18
Q

Osteogenesis imperfecta

A

type 1 mutation = brittle bones

19
Q

Scurvy

A

vit C deficiency = defective collagen

20
Q

How do enzymes lower activation energy?

A

Provide groups and better orientation

21
Q

Active site

A

specific, 3D, multiple weak interactions

22
Q

Vmax

A

Theoretical max rate of reaction

23
Q

Km

A

Michaelis constant- affinity

= k2 + k3 / k1

24
Q

Factor affecting rate of reaction

A
substrate concentration
enzyme concentration
temperature
pH
inhibitors
25
Q

Irreversible covalent modification

A

eg. serine nerve agonists

26
Q

Reversible competition

A

increases Km

27
Q

Irreversible competition

A

Lowers Vmax

28
Q

Cofactors..

A

metal ions (active sites) and coenzymes (carry reaction components)