Structure and Properties of Peptides Secondary structure in protein refers to regular folding of regions of the polypeptide chain linear sequence of amino acids joined together by peptide bond three dimensional arrangement of all amino acids in polypeptide chain protein made up of more than one polypeptide chain regular folding of regions of the polypeptide chain linear sequence of amino acids joined together by peptide bond three dimensional arrangement of all amino acids in polypeptide chain protein made up of more than one polypeptide chain ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Heme is the binding pocket of myoglobin and hemoglobin and is composed of negatively charged residues polar residues positively charged residues hydrophobic residues negatively charged residues polar residues positively charged residues hydrophobic residues ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides What is the effect of a decrease in pH on hemoglobin oxygen affinity? Increase affinity in muscle cell otherwise decrease No effect on oxygen affinity Increase in oxygen affinity Decrease in oxygen affinity Increase affinity in muscle cell otherwise decrease No effect on oxygen affinity Increase in oxygen affinity Decrease in oxygen affinity ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides What is the proportion of glycine residues in collagenous regions? Half One-fourth One-third One-tenth Half One-fourth One-third One-tenth ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The oxygen binding curves of hemoglobin and myoglobin are a consequence of the quaternary structure of hemoglobin both (a) and (b) allow maximum transfer of oxygen to the tissues are identical are a consequence of the quaternary structure of hemoglobin both (a) and (b) allow maximum transfer of oxygen to the tissues are identical ANSWER DOWNLOAD EXAMIANS APP
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