Chapter 4: Protein structure Flashcards

1
Q

Native fold

A

When protein molecules adopt a a specific 3D conformation based on the amino acid sequence

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2
Q

What does dynamic & marginally stable means?

A

Protein biological function depends on its 3d structure

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3
Q

The ______ 3D structure has the lowest energy with the maximum number of weak interactions

A

Native

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4
Q

What are the four levels of protein structure?

A
  1. Primary structure
  2. Secondary structure
  3. Tertiary structure
  4. Quaternary structure
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5
Q

What are the favorable interactions among proteins?

A
  1. Hydrophobic effect
  2. Hydrogen bonds between protein hydrogen bond donors and acceptors
  3. London dispersion
  4. Electrostatic interactions
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6
Q

Hydrophobic effect (predominant stabilizing force)

A

Clustered nonpolar groups form a hydrophobic core reducing highly ordered water shells

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7
Q

Hydrogen bonds between protein hydrogen bond donor & acceptors

A

Interactions with N & O to form hydrogen bonds along the peptide chain forms regular stable structures

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8
Q

London dispersion forces

A

Weak attraction between atoms contributes significant stability in protein’s interior

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9
Q

Electrostatic interactions

A

Strong interactions between permanently charged groups such as salt-bridges

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10
Q

Peptide group is what?

A

6 atoms that occupy the same plane

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11
Q

___________ character restricts conformation in either trans or cis configuration

A

Partial bond

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12
Q

___________ from backbone & R groups size/ limit a peptide formation

A

Partial bond

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13
Q

Most proteins peptide groups are _______ conformations to minimize steric conflict

A

trans

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14
Q

____________ plots show the distribution of the phi & psi angles

A

Ramachandran

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15
Q

What are the conformation angles in common secondary structures

A
  1. Beta sheets
  2. Alpha helix
  3. Collagen helix
  4. Left-handed alpha helix
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