CH 3 Flashcards

(17 cards)

1
Q

How do amino acids react to water

A

In pH 7 water, amino acids IONIZE
- it causes the amino group to act as a base & attracts a proton to form NH3+
- the carboxyl group then acts as an acid

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2
Q

why are the charges on the function groups of amino acids important

A

(1) They help amino acids stay in solution, where they can interact with one another and with other solutes,
(2) they affect the amino acid’s chemical reactivity.

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3
Q

Function of amino acids with side chains that have no functional groups

A
  • they consist solely of carbon & hydrogen atoms
  • rarely participate in chemical reactions
  • influence primarily depends on size & shape rather than reactivity
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4
Q

Hydrophilic R-groups

A

polar & electrically charged

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5
Q

Hydrophobic R-groups

A

nonpolar lacking charge & highly electronegative atoms capable of forming hydrogen bonds with water

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6
Q

acidic r-groups

A
  • has a negative charge & lost a proton
  • e.g. aspartate
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7
Q

basic r-groups

A
  • positive charge & picked up a proton
  • e.g. lysine
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8
Q

uncharged polar r-group

A
  • has highly electronegative oxygen that will form a polar covalent bond in the r group
  • e.g. serine
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9
Q

Why are peptide bonds unusually stable

A

the nitrogen can intermittently donate its pair of unshared valence electrons to the carbon in the C-N bond

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10
Q

How do R-groups affect each amino acid

A

size, shape, chemical reactivity, & solubility
- properties & function

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11
Q

secondary structures

A
  • H bonding occurs btwn oxygen on carbonyl (- charge) of one amino acid residue & the H (+ charge) on the amino group of another
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12
Q

dimer

A

proteins with 2 polypeptide subunits

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13
Q

macromolecular machines

A

a group of proteins, & possibly other nonprotein macromolecules, that assemble to carry out a particular function

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14
Q

does protein folding tend to be spontaneous

A

yes
- this occurs when a chain is placed in an aqueous solution

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15
Q

hydrophobic interactions with proteins

A

drive proteins to fold such that their nonpolar R-groups coalesce (join) in the interior
- increases entropy of the surrounding water
- folded molecule has less potential energy = more stable

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16
Q

molecular chaperones

A

a protein that facilitates the folding or refolding of a protein into its correct 3D shape
- heat-shock proteins
- attach to hydrophobic patches before aggregates can form

17
Q

prions

A
  • proteinaceous infectious particles
  • infectious particle that consists entirely of protein
  • adopt a normally folded shape & an infectious, often disease-causing shape
  • can bind normally folded prion proteins & cause them to adopt infectious shape