Structure and Properties of Peptides The oxygen binding curves of hemoglobin and myoglobin 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 are a consequence of the quaternary structure of hemoglobin are identical both (a) and (b) ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides In the β-pleated sheet 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 the polypeptide chain is fully extended All of these 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 two polypeptide chains, one α-chains and one β-chains five polypeptide chains, two α-chains and three β-chains four polypeptide chains, two α-chains and two β-chains six polypeptide chains, two α-chains and four β-chains two polypeptide chains, one α-chains and one β-chains five polypeptide chains, two α-chains and three β-chains four polypeptide chains, two α-chains and two β-chains ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides In deoxy hemoglobin (Hb), the Fe (II) is coordinated to four nitrogens of heme and to a water molecule two nitrogens of heme and to three His residues in Hb two nitrogens of heme and to three water molecules four nitrogens of heme, the proximal His, and a water molecule four nitrogens of heme and to a water molecule two nitrogens of heme and to three His residues in Hb two nitrogens of heme and to three water molecules four nitrogens of heme, the proximal His, and a water molecule ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The same peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala. was digested with chymotrypsin 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 Heme is the binding pocket of myoglobin and hemoglobin and is composed of negatively charged residues hydrophobic residues positively charged residues polar residues negatively charged residues hydrophobic residues positively charged residues polar residues ANSWER DOWNLOAD EXAMIANS APP
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