Structure and Properties of Peptides Secondary structure in protein refers to three dimensional arrangement of all amino acids in polypeptide chain linear sequence of amino acids joined together by peptide bond protein made up of more than one polypeptide chain regular folding of regions of the polypeptide chain three dimensional arrangement of all amino acids in polypeptide chain linear sequence of amino acids joined together by peptide bond protein made up of more than one polypeptide chain regular folding of regions of the polypeptide chain ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides What is the proportion of glycine residues in collagenous regions? One-third One-tenth One-fourth Half One-third One-tenth One-fourth Half ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The oxygen in hemoglobin and myoglobin is bound to lysine residues in the protein the iron atom in the heme group the nitrogen atoms on the heme histidine residues in the protein lysine residues in the protein the iron atom in the heme group the nitrogen atoms on the heme histidine residues in the protein ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Hemoglobin has quaternary structure and is made up of six polypeptide chains, two α-chains and four β-chains five polypeptide chains, two α-chains and three β-chains two polypeptide chains, one α-chains and one β-chains four polypeptide chains, two α-chains and two β-chains six polypeptide chains, two α-chains and four β-chains five polypeptide chains, two α-chains and three 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 Heme is the binding pocket of myoglobin and hemoglobin and is composed of polar residues negatively charged residues hydrophobic residues positively charged residues polar residues negatively charged residues hydrophobic residues positively charged residues 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 are identical both (a) and (b) allow maximum transfer of oxygen to the tissues are a consequence of the quaternary structure of hemoglobin are identical both (a) and (b) allow maximum transfer of oxygen to the tissues ANSWER DOWNLOAD EXAMIANS APP
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