BCHM 307 QUIZ 2 QUESTIONS WITH
VERIFIED ANSWERS
Hydrocarbons will always be (Hydrophilic/hydrophobic) - Answer-Hydrophobic
2 amino acids with sulfur - Answer-Methionine and Cystine
What is the first amino acid in all proteins - Answer-Methionine (Met, M)
What is the start codon? - Answer-Methionine (Met, M)
Three letter start codon - Answer-AUG
Only amino acid with a fused ring system, most proteins have atleast one, absorbs UV
light at 280nm - Answer-Tryptophan (Trp, N)
Only amino acid whose side chain loops back into its own back bone, produces kinks in
a polypeptide sequence - Answer-Proline (Pro, P)
Polar amino acids are often found where? Why? - Answer-in the active sites of enzymes
because they can facilitate chemical catalysis
can form disulfide bonds with itself, condensation reaction, can form interchain
crosslinks - Answer-Cystine (Cys, C)
OH group is key to being polar, other chemicals can covalently bond to the OH group -
Answer-Serine (Ser, S)
OH group is key to being polar, very prominent in nucleophiles - Answer-Threonine
(Thr, T)
Derivative of phenylalanine, precursor of amino acid derivatives that are
neurotransmitters
Polar, uncharged - Answer-Tyrosine (Tyr, Y)
Asparagine (Asn, N) side chain - Answer--CH2-C(=O)-NH2
Glutamine (Gln, Q) side chain - Answer--CH2-CH2-C(=O)-NH2
Asparagine and Glutamine are both (polar/nonpolar) (Charged/uncharged) - Answer-
polar, uncharged
, Nitrogen containing ring, polar/uncharged, doesn't fit into a group well - Answer-
Histidine (His, H)
Both are definitely charged and have long side chains with positively charged amine
groups - Answer-Lysine (Lys, K) and Arginine (Arg, R)
The pK of the nitrogen ring of Histidine is - Answer-6
analogous to asparagine and Glytamine, but these both have carboxylate groups
Low pK, pretty much always deprotonated - Answer-Aspartate and Glutamate
Amino acids are linked via _________. - Answer-condensation (dehydration) reactions
Amino acids are polymerized via - Answer-a peptide bond
A peptide bond it created when - Answer-amino acid #1 (the carboxylic acid) reacts with
the amine group of amino acid #2
4 levels of protein structure - Answer-1. Primary
2. Secondary
3. Tertiary
4. Quaternary
Primary structure definition - Answer-The sequence of amino acid residues
(Glu-Ser-Phe-Gly-Asp-)
Secondary structure definiton - Answer-the localized conformation of the polypeptide
backbone
What protein structure?: first three dimensional folding - Answer-Secondary
What protein structure?:
represented by space filling, "Ribbon Diagram", & "Ball and Stick" - Answer-Secondary
What protein structure?:
alpha helix and beta sheet - Answer-Secondary
H bonds form in an alpha helix between - Answer-the carbonyl oxygen and the amino
hydrogen
What protein structure?:
a folded polypeptide assumes a shape with a hydrophilic surface and a hydrophobic
core - Answer-Tertiary structure
VERIFIED ANSWERS
Hydrocarbons will always be (Hydrophilic/hydrophobic) - Answer-Hydrophobic
2 amino acids with sulfur - Answer-Methionine and Cystine
What is the first amino acid in all proteins - Answer-Methionine (Met, M)
What is the start codon? - Answer-Methionine (Met, M)
Three letter start codon - Answer-AUG
Only amino acid with a fused ring system, most proteins have atleast one, absorbs UV
light at 280nm - Answer-Tryptophan (Trp, N)
Only amino acid whose side chain loops back into its own back bone, produces kinks in
a polypeptide sequence - Answer-Proline (Pro, P)
Polar amino acids are often found where? Why? - Answer-in the active sites of enzymes
because they can facilitate chemical catalysis
can form disulfide bonds with itself, condensation reaction, can form interchain
crosslinks - Answer-Cystine (Cys, C)
OH group is key to being polar, other chemicals can covalently bond to the OH group -
Answer-Serine (Ser, S)
OH group is key to being polar, very prominent in nucleophiles - Answer-Threonine
(Thr, T)
Derivative of phenylalanine, precursor of amino acid derivatives that are
neurotransmitters
Polar, uncharged - Answer-Tyrosine (Tyr, Y)
Asparagine (Asn, N) side chain - Answer--CH2-C(=O)-NH2
Glutamine (Gln, Q) side chain - Answer--CH2-CH2-C(=O)-NH2
Asparagine and Glutamine are both (polar/nonpolar) (Charged/uncharged) - Answer-
polar, uncharged
, Nitrogen containing ring, polar/uncharged, doesn't fit into a group well - Answer-
Histidine (His, H)
Both are definitely charged and have long side chains with positively charged amine
groups - Answer-Lysine (Lys, K) and Arginine (Arg, R)
The pK of the nitrogen ring of Histidine is - Answer-6
analogous to asparagine and Glytamine, but these both have carboxylate groups
Low pK, pretty much always deprotonated - Answer-Aspartate and Glutamate
Amino acids are linked via _________. - Answer-condensation (dehydration) reactions
Amino acids are polymerized via - Answer-a peptide bond
A peptide bond it created when - Answer-amino acid #1 (the carboxylic acid) reacts with
the amine group of amino acid #2
4 levels of protein structure - Answer-1. Primary
2. Secondary
3. Tertiary
4. Quaternary
Primary structure definition - Answer-The sequence of amino acid residues
(Glu-Ser-Phe-Gly-Asp-)
Secondary structure definiton - Answer-the localized conformation of the polypeptide
backbone
What protein structure?: first three dimensional folding - Answer-Secondary
What protein structure?:
represented by space filling, "Ribbon Diagram", & "Ball and Stick" - Answer-Secondary
What protein structure?:
alpha helix and beta sheet - Answer-Secondary
H bonds form in an alpha helix between - Answer-the carbonyl oxygen and the amino
hydrogen
What protein structure?:
a folded polypeptide assumes a shape with a hydrophilic surface and a hydrophobic
core - Answer-Tertiary structure
