Lecture 5 Protein Structure Flashcards

1
Q

3 Methods to look at protein structure

A
  1. X-ray crystallography
  2. NMR
  3. Circular Dichoasism Spectroscopy
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2
Q

X-ray Crystallography

A

Good for conformational proteins

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3
Q

NMR and protein structure

A

Looking at soluble proteins, better example of how they will be in tissues

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4
Q

Circular Dichoasism Spectroscopy

A

Looks at tendency to bend light in a circular pattern. Determines secondary structure.
Can get % of alpha helices, beta strands and random coil

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5
Q

Primary

A

Long chain

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6
Q

Secondary

A

How chains twist

*alpha helices and beta strands

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7
Q

Tertiary

A

Structure of protein and how it relates to itself

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8
Q

Quaternary

A

Has to have more than one chain to have quaternary

Reason for this 1. stability 2. regulation of biological activity

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9
Q

2 Reasons for quaternary structure

A
  1. Stability - important for all proteins

2. Regulation of biological activity

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10
Q

What is necessary for quaternary structure

A

More than one chain

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11
Q

Regulatory domain

A

Determines what protein will do, has repetitive components

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12
Q

N-terminus

A

L side of polypeptide ring

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13
Q

C-terminus

A

R side of polypeptide ring

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14
Q

Main chain

A

backbone

Has ability to bond every couple of bondings

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15
Q

This defines secondary structure

A

H bonding

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16
Q

Resonance gives peptide bond

A

Partial double bond characteristics

Can’t rotate

17
Q

Trans

A

Opposite side

18
Q

Cis

A

Same side

19
Q

2 Torsion Angles

A

Phi and psi

20
Q

Torsion angle between N-C is

A

Phy

21
Q

Torsion angle between C to carboxyl C

A

Psi

22
Q

This lists the phi and psi angles

A

Ramachandran Diagram

23
Q

Most alpha helices are

A

R handed

24
Q

R groups on alpha helices

A

Project to outside

25
Q

Beta strands

A

Extended secondary structure, interact with each other to create a sheet
Backbone H bonding
R groups project from top and bottom of sheet

26
Q

R groups on beta sheets

A

Project from top and bottom of sheet