Protein Structures 1 Flashcards

1
Q

Levels of Proteins Structure

A

Primary Structure, Secondary. Tertiary, Quaternary

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2
Q

Primary Structure

A

complete set of covalent bonds within a protein

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3
Q

Why can’t a peptide bond form as by definition?

A

It requires specific activation over overcome energy barrier for reaction and need helps from enzymes to form the bond. It doesn’t happen spontaneously.

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4
Q

Why is a peptide bond planar and rigid?

A

The peptide C-N bond has a partial double-bond character (estimated at 40%
under typical conditions, partial sharing of two pairs of electrons between O and
N).

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5
Q

resonance

A

delocalization of bonding electrons over more than one chemical
bond

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6
Q

Is peptide bond normally in trans or cis configurtion?

A

trans configuration

except proline which makes the aa constrained

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7
Q

what does “complete description of the covalent bond network” mean?

A

this is talking about the covalent bonds between amino acid at the C-N bond and between side chain atoms

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8
Q

backbone atom pattern

A

-N-Ca-C-N-Ca-C-N-Ca-C-N-Ca-C-

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9
Q

Ramachandran Plot

A

graph that helps scientists understand the angles in the backbone of a protein

x-axis (horizontal) shows one type of angle, called ϕ (phi)

y-axis (vertical) shows another type of angle, called ψ (psi)

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10
Q

phi

A

C - N - C-alpha - C
ϕ

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11
Q

psi

A

N - C-alpha - C - N
ψ

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12
Q

backbone dependent

A

phi & psi

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13
Q

backbone independent

A

omega

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14
Q

Peptide bonds are in WHAT configuration? Why?

A

trans because trans in not constrained while cis is.

A constrained configuration makes it difficult for the protein to be flexible and move.

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15
Q

disulfide bond

A

strong covalent bond formed between two sulfur atoms of two cysteine amino acids (and produces a cystine)

It stablizises a protein which makes it rigid and less likely to unfold (like a glue)

Seen in enzymes

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