1. The side chain of tyrosine is considered to be polar because even though it is reminiscent of phenylalanine it also has two types of atoms that have large differences in electronegativity with asymmetry at the terminus.
a.) True
b.) False
2. Which of these changes in primary structure will be certain to cause a loss of protein activity?
a.) Asp to Glu
b.) His to Lys
c.) Trp to Ser
d.) Gly to Pro
e.) Not enough information is given since any one of these changes could be severe depending on the context of the situation
3.The difference between fetal and adult hemoglobin with regard to oxygen binding occurs because fetal hemoglobin has an amino acid substitution in one of its chains that results in a histidine (adult version) being replaced by a serine (fetal version).
a.) True
b.) False
4. What will likely happen if the side chains of aspartate and histidine at pH 5 are next to each other in a polypeptide chain?
a.) The side chains of these amino acids will be uncharged and there will be no electrostatic effect.
b.) The side chains of these amino acids will be charged and they will attract each other.
c.) The side chains of these amino acids will be charged and they will repel each other.
d.) Not enough information is given to determine the effect.
5. A beta pleated sheet:
a.) can occur between two different polypeptide chains
b.) can be formed by either intramolecular or intermolecular hydrogen bonds
c.) can only form when cysteines form disulfide bridges within this structure
d.) forms when side chains of D and E attract each other
e.) both a and b
1. The side chain of tyrosine is considered to be polar because even though it is reminiscent of phenylalanine it also has two types of atoms that have large differences in electronegativity with asymmetry at the terminus.
a.) True
b.) False
2. Which of these changes in primary structure will be certain to cause a loss of protein activity?
a.) Asp to Glu
b.) His to Lys
c.) Trp to Ser
d.) Gly to Pro
e.) Not enough information is given since any one of these changes could be severe depending on the context of the situation
3.The difference between fetal and adult hemoglobin with regard to oxygen binding occurs because fetal hemoglobin has an amino acid substitution in one of its chains that results in a histidine (adult version) being replaced by a serine (fetal version).
a.) True
b.) False
4. What will likely happen if the side chains of aspartate and histidine at pH 5 are next to each other in a polypeptide chain?
a.) The side chains of these amino acids will be uncharged and there will be no electrostatic effect.
b.) The side chains of these amino acids will be charged and they will attract each other.
c.) The side chains of these amino acids will be charged and they will repel each other.
d.) Not enough information is given to determine the effect.
5. A beta pleated sheet:
a.) can occur between two different polypeptide chains
b.) can be formed by either intramolecular or intermolecular hydrogen bonds
c.) can only form when cysteines form disulfide bridges within this structure
d.) forms when side chains of D and E attract each other
e.) both a and b
