Structure and Properties of Peptides Heme is the binding pocket of myoglobin and hemoglobin and is composed of hydrophobic residues polar residues positively charged residues negatively charged residues hydrophobic residues polar residues positively charged residues negatively charged residues ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides If the F and Y angles of each peptide unit in a protein are known, which of the following may also be determined? Complete quaternary structure Complete tertiary structure Complete secondary structure Thermodynamic stability Complete quaternary structure Complete tertiary structure Complete secondary structure Thermodynamic stability ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides What is the effect of a decrease in pH on hemoglobin oxygen affinity? Increase in oxygen affinity No effect on oxygen affinity Decrease in oxygen affinity Increase affinity in muscle cell otherwise decrease Increase in oxygen affinity No effect on oxygen affinity Decrease in oxygen affinity Increase affinity in muscle cell otherwise decrease ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides In the β-pleated sheet the polypeptide chain is fully extended All of these adjacent polypeptide chains can either be parallel or antiparallel hydrogen bonds are formed between the peptide bonds the polypeptide chain is fully extended All of these adjacent polypeptide chains can either be parallel or antiparallel hydrogen bonds are formed between the peptide bonds ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala, was digested with cyanogen bromide (CNBr) to produce: Val-Lys-Glu-Met + Ser-Trp-Arg-Ala Val-Lys-Glu + Met-Ser-Trp-Arg-Ala Val-Lys + Glu-Met-Ser + Trp-Arg-Ala Val-Lys-Glu-Met-Ser-Trp + Arg-Ala Val-Lys-Glu-Met + Ser-Trp-Arg-Ala Val-Lys-Glu + Met-Ser-Trp-Arg-Ala Val-Lys + Glu-Met-Ser + Trp-Arg-Ala Val-Lys-Glu-Met-Ser-Trp + Arg-Ala ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The oxygen binding curves of hemoglobin and myoglobin allow maximum transfer of oxygen to the tissues both (a) and (b) are a consequence of the quaternary structure of hemoglobin are identical allow maximum transfer of oxygen to the tissues both (a) and (b) are a consequence of the quaternary structure of hemoglobin are identical ANSWER DOWNLOAD EXAMIANS APP
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