Structure and Properties of Peptides Disulfide bonds most often stabilize the native structure of intracellular proteins hydrophobic proteins extracellular proteins dimeric proteins intracellular proteins hydrophobic proteins extracellular proteins dimeric proteins ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides When pO2 = Kd of myoglobin, the fractional saturation (YO2) is about 1.7 0.1 0.5 0.9 1.7 0.1 0.5 0.9 ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Hemoglobin has quaternary structure and is made up of five polypeptide chains, two α-chains and three β-chains six polypeptide chains, two α-chains and four β-chains two polypeptide chains, one α-chains and one β-chains four polypeptide chains, two α-chains and two β-chains five polypeptide chains, two α-chains and three β-chains six polypeptide chains, two α-chains and four β-chains two polypeptide chains, one α-chains and one β-chains four polypeptide chains, two α-chains and two β-chains ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The major element of secondary structure in myoglobin and hemoglobin is the P-strand the a-helix the reverse turn All of these the P-strand the a-helix the reverse turn All of these ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides What is the effect of a decrease in pH on hemoglobin oxygen affinity? Decrease in oxygen affinity No effect on oxygen affinity Increase in oxygen affinity Increase affinity in muscle cell otherwise decrease Decrease in oxygen affinity No effect on oxygen affinity Increase in oxygen affinity Increase affinity in muscle cell otherwise decrease ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Which of the following is an example of tertiary structure in a protein? An a-helix A globular domain A multimeric protein A P-pleated sheet An a-helix A globular domain A multimeric protein A P-pleated sheet ANSWER DOWNLOAD EXAMIANS APP
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