Proteins Structure and Function Flashcards

1
Q

In what level of protein folding does hydrogen bonding occur

A

Secondary

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2
Q

amino acids are joined by what kind of reaction

A

dehydration reaction

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3
Q

synthesis of protein occurs from what end of amino acid to what end

A

starts with amino side on the left and finishes with the carboxyl end on the right side

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4
Q

Describe the planes of peptide bond

A
  • carbon and nitrogen form planes
  • rotation can occur around bonds attached to alpha carbon
  • side chains alternate above and below chain
  • peptide bond is a resonance between two structures
  • results in negative charge on oxygen and positive charge on nitrogen
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5
Q

Is the cis or trans configuration favored

A

Trans because the side chains are bulky and would bump into each other if they were on the same side of the chain

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6
Q

which amino acid cannot be in alpha helix

A

Proline due to its rigid structure, if inserted it would end the alpha helix

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7
Q

describe the bonding of an alpha helix

A

oxygen atom of a carbonyl binds to a hydrogen through hydrogen binding that is attached to a nitrogen 4 amino acids down in the chain.

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8
Q

describe how our body deals with proline in a protein structure

A

it can enzymatically switch it from trans to cis or vice versa to get it to fit into the growing peptide chain,

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9
Q

where are r groups positioned in helix

A

on the outside of the peptide so it can interact with other r groups or external environment

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10
Q

parallel and antiparallel beta pleated sheets

A

parallel means the amino terminus and carboxyl terminus are running in the same direction as far as the planes whereas antiparallel means they are running in the opposite plane or direction

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11
Q

What 3 bonds hold the secondary structures together to help form tertiary structures

A

hydrogen bonds, hydrophobic interactions, and ionic bonds

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12
Q

What type of bonds are in tertiary structure

A

sulfhydryl (S-S) bonds which are a type of covalent bond

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