Protein Motifs Flashcards

1
Q

What is a protein motif

A

Arrangements of limited numbers of secondary structure elements
Form part of larger regions of proteins-domains
In multi-domain proteins each domain has a role

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2
Q

What are ß-α-ß motifs

A

Found in almost every structure that contains parallel b-sheet
a-helix connects the C-terminus of one b-strand with the N-terminus of a second
b-a-b contains two b-strands, two loop regions and one a-helix.
Can be found in larger, repeating domains
Found in repeating units in proteins

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3
Q

What are some different types of protein motifs

A

Helix-loop-helix
Zinc finger
EF hand motif
Greek key motif
b-a-b motif
Leucine rich motif
Rossman fold

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4
Q

What is y- crystallin

A

Y-crystallin protein is in lens of the eye
Responsible in part for transparency and refractive power
Contains 2 domains
Each domain contains two Greek key motifs

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5
Q

what is the structure of a pyruvate uinase

A

530 amino acids
Tetramer, only a monomer is shown
4 different domains

N-terminal domain key in oligomer formation
a/b barrel is core functional domain

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6
Q

Why are proteins multi domain

A

One suggestion is that it makes evolving new proteins easier- Easier than single point mutations
A domain in one protein can be transposed to another protein-should do the same job
Multidomain organisation makes it easy to introduce control and regulation

Multidomain construction simplifies folding and assembly
Stabilizes the protein
Large single domain protein would take a long time to fold
Domains fold independently

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7
Q

What can domains be

A

Domains can be a-helical, b-strand or a mixture of both.

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8
Q

Why are oligomers important

A

Important for function
Stabilises proteins
Cooperativity

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9
Q

What are the characteristics of protein motifs

A
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10
Q

What is a helix-loop-helix motif

A
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11
Q

What do transcription factors do

A
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12
Q

What is the zinc finger domain

A
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13
Q

What is a 4 helix bundle

A
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14
Q

What are the 4 different ways for a 4 helix bundle to be arranged

A
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15
Q

What is the EF hand motif

A
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16
Q

What is a Greek key motif

A
17
Q

How can motifs be identified

A

Can be identified by sequencing primary structure
Sequencing a motif can allow identification of other EF hand hoop motifs in the absence of structure

18
Q

Why are motifs important

A

They’re important for fold and function
Proteins with similar functions will contain the same motif

19
Q

What is the problem with a protein having a large loop

A

Less stability

20
Q

Why are there many glycine residues in active site regions of proteins

A

It makes the active site more flexible

21
Q

how do you compare the structure of two domains

A

Superposition allows comparisons of different domains ( overlaying the structures in 3D/ putting them ontop of each other)
Root mean square deviation- gives a quantitative measure of how similar the two protein structures are

22
Q

What are domains in proteins

A

Domains are combined to make proteins