Final Flashcards

1
Q

what is electronegativity

A

a measure of the force of an atoms attraction for electrons it shares in a chemical bond with another atom

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2
Q

a compound that contains both an amino group and a carboxyl group

A

amino acid

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3
Q

what gives identity to an amino acid

A

the R group

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4
Q

pKa value of the carboxylate group

A

2.3

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5
Q

pKa value of the amino group

A

9.5

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6
Q

what determines the 3D conformation of a protein

A

its primary structure

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7
Q

hemoglobin associated with sickle cell anemia is an example of what

A

how a change in just one amino acid in a proteins primary structure can alter biological function

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8
Q

where does free rotation occur in the secondary structure of a protein

A
  1. between the alpha carbon and amino nitrogen
  2. between the alpha carbon and carboxyl carbon
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9
Q

Why is there no rotation around the omega (ω) bond in a peptide?

A

the bond between the carbonyl oxygen and the amide nitrogen has partial double bond character due to a small electric dipole

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10
Q

where do all R groups point from the alpha helix

A

outward; they are found on the outside of the helical spiral

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11
Q

where does each carbonyl oxygen of the peptide bond to

A

forms a hydrogen bond with the amide hydrogen (N–H) of the fourth amino acid ahead in the sequence.

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12
Q

what stabilizes an alpha helix

A

the hydrogen bonds that run parallel to the axis

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13
Q

what amino acids are common in alpha helices

A

alanine, leucine and methionine

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14
Q

which amino acid is known as a helix breaker

A

proline

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15
Q

how does proline disrupt an alpha helix

A

creates a bend due to its cyclic structure and has no amino hydrogens for bonding

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16
Q

which amino acids would cause steric crowding due to the proximity of bulky side chains

A

ser, val, leu, ile, thr, cys and asn

17
Q

where do the C=O—-H-N bonds lie in an alpha helix

A

parallel to the helical axis

18
Q

where do the C=O—-H-N bonds lie in an beta pleated sheet

A

between adjacent sheets and perpendicular to the direction of the sheet

19
Q

alpha helices and beta pleated sheets are apart of what structure

20
Q

when do beta turns occur

A

when the peptide forms a tight loop with the carbonyl oxygen forming a hydrogen bond with the amide proton of the amino acid 3 positions down the chain

21
Q

what amino acids are commonly found in beta turns

A

glycine and proline

22
Q

why is proline common in beta turns

A

the cyclic amino acid produces a bend or kink in the amino acid sequence

23
Q

why is glycine common in beta turns

A

small and easily adaptable to the steric constraints of the turn

24
Q

types of supersecondary structures

A

beta-alpha-beta
alpha-alpha
beta-meander
greek key
beta-barrel

25
what are the two major classes of tertiary structure
fibrous and globular proteins
26
what are the noncovalent interactions in tertiary structure
-hydrogen bonding between polar side chains -hydrophobic interactions between nonpolar side chains =electrostatic attraction between side chains of opposite charge -electrostatic repulsion between side chains of like charge
27
what is the covalent interaction of tertiary structure
disulfide bonds between side chains of cysteines
28
what amino acids are common in beta pleated sheets
glycine, alanine and serine
29
examples of fibrous proteins
keratin of hair and wool, collagen of connective tissue
30
an important constituent of connective tissue; long chains of glycine and proline with a left handed helix
collagen
31
what are ways to denature a protein
1. heat 2. large changes in pH (alters side chains) 3. detergents like SDS (disrupt hydrogen bonding) 4. urea or guanidine (disrupts hydrogen bonding) 5. beta-mercaptoethanol (reduces disulfide bonds)
32