Protein Structure Flashcards

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1
Q

Definition of primary

A

Sequence of AA in peptide chain

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2
Q

Definition of secondary

A

Folding of chain into a helix/b pleated sheets

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3
Q

Definition of tertiary

A

Peptide chain folds upon itself

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4
Q

Definition of quaternary

A

Folded peptide chains joined together

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5
Q

Functional groups on amino acids

A

Amino

Carboxyl

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6
Q

Reactions between amino acids and dipeptides

A

Dehydration/synthesis

Acid hydrolysis

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7
Q

Properties of peptide bonds

A
Has characteristics of C=C
However, C-N bond length shorter than expected, no rotation, trans groups
Partial -ve on O
Partial +ve on N
HB can form between 2 polar AA
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8
Q

Direction of polypetides

A
NH3+ = N terminal
COO- = C terminal
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9
Q

Covalent linkages, post translation modification

A

Disulphide bridges Cys-Cys
Glycosylation
Phosphorylation
Methylation via NH2 groups

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10
Q

How does glycosylation work

A

Sugars bind to OH of Thr, Her

Sugars bind tp NH2 of Asn

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11
Q

How does phosphorylation affect proteins

A

Cell signal transduction

Change in enzyme activity

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12
Q

How does methylation via NH2 groups affect proteins

A

Histones and gene expression

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13
Q

Properties of a helices

A

HB in same PP chain, not between side chains
HB formed between COOH, NH2 of every 4th peptide
RH helix
Turn stabilized by HB
R groups on outside
Rigid cylinder, support for protein

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14
Q

Properties of b pleated sheets

A

Linear peptide chains
HB between chains holds strands in B sheet
Side chains in each strand alternately lie above and below sheet plane

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15
Q

Properties of collagen triple helix

A

3 chains with HB between chains
LH helix
Gly, Pro, hydroxypro, repeated sections

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16
Q

Forces that stabilize protein structure

A
Covalent (disulphide bridges)
HB
IB
LF
Hydrophobic effects
17
Q

How do HB work

A

2 delta -ve atoms compete for the same H atom

Between H and lone electron pair on O, N

18
Q

How do IB work

A

Between charged side chains
Asp, Glu COO-
Arg, Lys NH3+

19
Q

How do LF work

A

Sum of attractive/repulsive forces between molecules

Unequal distribution of electrons results in instantaneous dipoles

20
Q

How do hydrophobic effects work

A

Fold in a way to minimize contact with water

Cannot form HB due to hydrophobic R groups

21
Q

How to disrupt protein structure and function

A

pH
Temperature
Ionic strength

22
Q

How are proteins folded

A

All proteins have different structures but only 1 is functional
Primary structure encodes pathway that leads to final structure which is most stable

23
Q

What can misfiled proteins result in

A

Mutations can cause a protein to fold incorrectly

If not folded properly, stable protein aggregates can form

24
Q

Neurological symptoms in Creutzfeldt Jakob disease

A
Walking difficulties
Slurred speech
Numbness
Dizziness
Visual problems
25
Q

Psychological symptoms of Creutzfeldt Jakob disease

A
Severe depression
Withdrawal
Anxiety
Irritability
Insomnia
26
Q

What happens to the normal prion proteins

A

Normal cellular prion proteins become pathogenic prion proteins

Pathogenic prions can form fibril aggregates

27
Q

Compare the structures of prion proteins

A

PrPc
a helix, no b sheets
Susceptible to proteolysis

PrPsc
less a helix, b sheet present
Protease resistant

Both have the same AA sequence