Protein Structure Flashcards

1
Q

What are the properties of a peptide bond?

A

partial double bond character; dipole moment, trans-configuration, uncharged but polar, rigid and planar

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2
Q

What is the geometry of a peptide bond?

A

planar trans configuration

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3
Q

native conformation

A

the tertiary structure of a protein

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4
Q

bends

A

beta-bends are seen in beta-sheets. They function to reverse the direction of the polypeptide chain; usually composed of 4 AA

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5
Q

What is primary structure of a protein?

A

amino acid residues

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6
Q

What is secondary structure of a protein?

A

3-dimensional shape

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7
Q

What is tertiary structure of a protein?

A

folding of 3-dimensional structure within the same polypeptide

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8
Q

What is quaternary structure of a protein?

A

assembly of multiple polypeptides

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9
Q

Compare alpha helix and beta helix

A

Alpha: helical, 3.6 residues/turn, intrachain H-bonding;
Beta: pleated, all peptides involved in H-bonding; parallel or anti-parallel

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10
Q

Define supersecondary structure

A

folding of secondary structure into small, discrete, commonly-observed aggregates of secondary structure

examples:
beta-alpha-beta loop
alpha-alpha corner
beta-barrel

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11
Q

genetic disease results from abnormalities in this structure of a protein

A

Primary structure

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12
Q

Intramolecular disulfide bridge vs Intermolecular disulfide bridge

A

intramolecular is between cysteines on same polypeptide; intermolecular is between cycteines on different polypeptides

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13
Q

What process can be used to break peptide bonds?

A

Acid hydrolysis

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14
Q

What reagent is used in sequencing of peptides and what is its function?

A

Phenyisothiocynate (Edman’s reagent); it labels the N-ternminal amino, which weakens the peptide bond between the first and second amino.

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15
Q

What stabilizes the secondary structure of a protein?

A

H-bonds

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16
Q

What are the characteristics of a globular protein?

A
  • various secondary structures
  • spherical shape
  • good water solubility
  • catalytic/regulatory/transport role (dynamic metabolic function)
17
Q

What are the characteristics of a fibrous protein?

A
  • one dominating secondary structure
  • long narrow rod-like structure
  • low water solubility
  • role in determining tissue/cellular structure and function
18
Q

What kinds of interactions are involved in maintaining tertiary structures?

A
  • H-bonds
  • Disulfide bonds
  • Hydrophobic interactions (van der waals)
  • electrostatic interactions (ionic &/or polar)
19
Q

What are domains?

A

fundamental, funtional and 3-D structural units of polypeptides

20
Q

This plays a role in folding of proteins during their synthesis

A

Chaperones

21
Q

What are some ways to denature a protein?

A
  • Heat
  • Organic Solvents
  • Mechanical Shearing
  • Heavy Metals
  • Detergents
  • Chaotropic Agents
22
Q

What enzyme has the ability to revert back to its original tertiary structure after denaturation?

A

Ribonuclease