Determinants of Protein Structure Flashcards

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1
Q

What is the 5th level of protein structure?

A

supramolecular (many protein subunits and complexes)

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2
Q

What is the levinthal paradox and what does it assume?

A

the shape of a protein is specified by its amino acid sequence
-assumes that each amino acid backbone can be in 3 conformational states

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3
Q

How must proteins fold?

A

in pre-arranged pathways and in a cooperative manner

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4
Q

What restricts the number of protein shapes that can be made?

A
  • chemical properties of atoms
  • peptide bonds can only be formed in few orientations
  • non-covalent bonds/interactions between amino acid side chains constrain the folding of a protein
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5
Q

What are van Der Waals attractions?

A

small charge differences caused by electron cloud fluctuating causing attractions or repulsions

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6
Q

What amino acid do disulphide bridges form between?

A

cysteine

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7
Q

How do disulphide bridges form?

A

when the sulfhydryl groups on cysteine are oxidised a disulphide bridge can form

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8
Q

What do non-covalent interactions dictate?

A

geometry and specificity

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9
Q

Describe the structure of the leucine zipper

A

The α-helices form a leucine residue at every second turn. These form a hydrophobic region running down one side of the helix

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10
Q

In protein folding, what is ΔG equal to?

A

the energy released or (required) when a protein folds into a native conformation

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11
Q

What is the equation for ΔG in protein folding?

A

ΔG= ΔH-T ΔS

ΔH= energy released due to non-covalent interactions
ΔS =change in molecular freedom
T= temp (K)

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12
Q

How can water effect the energetics of protein folding?

A
  • In an unfolded protein, water forms hydration sphere around hydrophobic amino acid side chains, as the water is ordered the entropy of the system is decreased
  • Hydrophobic interactions between amino acid side chains release the water from the hydration spheres
  • The water molecules therefore gain entropy as they are more disorganised so the entropy of the system (protein + solvent) increases
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13
Q

Does breaking non-covalent interactions release energy?

A

no it requires energy

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14
Q

In protein folding is ΔH usually +ve or -ve?

A

-ve

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