3D Structure of Proteins Flashcards

1
Q

4 Interactions in Proteins

A
  1. Hydrophobic Effect
  2. Hydrogen Bonds: lead to alpha helix and beta sheet structures
  3. London Dispersion: Weak interactions between atoms contributes to stability of interior of the protein
  4. Electrostatic Interactions: Strong interactions
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2
Q

What are the repeating atoms in the peptide backbone

A

N-C-C

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3
Q

Characteristics of the peptide bond

A
  • Planar
  • Polar
  • Rigid
  • Limited rotation around peptide bond
  • Behaves like a double bond
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4
Q

what bond is the peptide bond (atom wise)

A

C-N bond

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5
Q

Why is rotation around the peptide bond not permitted

A

Due to the resonance structure

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6
Q

Rotations around what bonds are permitted

A

Rotations around bonds connected to the alpha carbon are permitted:
* The alpha carbon - carbon bond (carbonyl carbon bond)
* The alpha carbon - nitrogen bond (amide nitrogen bond)

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7
Q

What does secondary structure refer to

A
  1. Local spatial arrangement
  2. Interactions within the polypeptide backbone
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8
Q

What are both alpha helices and beta sheets stabilised by

A

hydrogen bonds

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9
Q

What is irregular arrangement of the polypeptide chain called

A

Random coil

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10
Q

Which AAs are strong helix formers

A

Alanine (Ala)
Leucine (Leu)

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11
Q

What AAs are helix breakers and why (2)

A
  1. Proline (Pro): the rotation around the alpha carbon - nitrogen bond is impossible
  2. Glycine (Gly): the tiny R group supports other conformations (R group = H)
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12
Q

What creates a pleated sheet like structure

A
  1. The planarity of the peptide bond
  2. The tetrahedral geometry of the alpha carbon
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13
Q

What are beta sheets held together by

A

The hydrogen bonding of amide and carbonyl groups of the peptide bond from opposite strands

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14
Q

Characteristic of the h. bonds in parallel beta sheets

A

The hydrogen bonds between strands are bent and therefore weaker

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15
Q

Characteristic of the h. bonds in antiparallel beta sheets

A

The h. bonds between sheets are linear (straight) and therefore stronger

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16
Q

What AAs are common in beta turns

A

Proline & Glycine

17
Q

What does tertiary structure refer to

A

the overall 3D spatial arrangement of atoms in a protein

18
Q

what is the tertiary structure stabilised by

A

Multiple weak interations between AA side chains:
* Mostly hydrophobic and polar interactions
* Can be stabilised by disulphide bonds

19
Q

Structure of collagen (a fibrous protein)

A
  • Triple alpha helix coming together into a collagen fibril
  • Triple helices crosslinked to form collagen fibrils
  • Triple helix gives rigidity
20
Q

What is the structre of silk fibroin

A

Antiparallel beta sheet structure results in soft, flexible filaments

21
Q

How is the quaternary structure formed

A

The assembly of individual polypeptides into a larger functional cluster

22
Q

4 ways proteins can be denatured

A
  1. Heat/cold
  2. Extremes of pH
  3. Organic solvents
  4. Chaotropic agents: e.g: urea
23
Q

Function of chaperones in protein folding

A

Aid in folding protein into its native conformation.
They prevent misfolding & aggregation of unfolded peptides.
(Disaggregation, remodeling, folding)