Protein Levels Flashcards

1
Q

what is the primary level

A

sequence of amino acids in backbone

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2
Q

what is the secondary level

A

localised organisation of backbone

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3
Q

what are motifs

A

regular combination of secondary structure

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4
Q

what are domains

A

a functional unit of protein

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5
Q

what are teritary levels

A

overall shapes of protein

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6
Q

what are quaternary levels

A

interactions between more than one polypeptide to form multimers

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7
Q

what do sequences of amino acids fold into

A

alpha and beta sheets due to hydrogen bonding between N-H and C=O atoms

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8
Q

what is the alpha helix

A

H-bonds form between 4th amino acids

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9
Q

what is the beta sheet

A

H-bonds form between amino acids in different chains, can be parallel or anti-parallel

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10
Q

how are motifs formed

A

alpha + beta + other features = motifs

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11
Q

what is a helix-loop-helix

A

held together by weak interactions between mineral calcium and amino acids

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12
Q

what is the zinc-finger

A

2 B strands and alpha helix held by interactions with zinc

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13
Q

what is a coiled-coil

A

common in fibrous proteins and formed in alpha helixes with more hydrophobic residues

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14
Q

what gives overall structure

A

secondary structures + motif or domain = overall structure

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15
Q

what is an example of a domain

A

antibody variable domain

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16
Q

what are prosthetic groups

A

small molecules from vitamins and minerals that give proteins extra functions

17
Q

what is retinol

A

found in purple-light sensitive proteins and comes from Vitamins A and is surrounded by a cage of alpha helixes

18
Q

what are multimers

A

multiple proteins assembled together

19
Q

what does changing the position of the binding site cause

A

long fibres/rings generate from the same protein

20
Q

proteins with the most interactions at the binding site mean what

A

interact most stably

21
Q

why is quaternary structure called alpha2beta2

A

4 subunits, fall into 2 types alpha or beta and these have different territory shape

22
Q

what are conformational changes

A

these are important for protein function and are initiated by binding of other molecules. They change from one stable folded shape to other