Structure and Properties of Peptides The major element of secondary structure in myoglobin and hemoglobin is All of these the P-strand the reverse turn the a-helix All of these the P-strand the reverse turn the a-helix ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The peptide bond in proteins is is planar because of steric hinderance usually cis unless proline is the next amino acid only found between proline residues usually trans unless proline is the next amino acid is planar because of steric hinderance usually cis unless proline is the next amino acid only found between proline residues usually trans unless proline is the next amino acid ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The nature of peptide bond can be best explained as Hydrogen bond Van der waals force partial double bond truly double bond Hydrogen bond Van der waals force partial double bond truly double bond ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The oxygen in hemoglobin and myoglobin is bound to the iron atom in the heme group lysine residues in the protein histidine residues in the protein the nitrogen atoms on the heme the iron atom in the heme group lysine residues in the protein histidine residues in the protein the nitrogen atoms on the heme ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides What is the proportion of glycine residues in collagenous regions? One-fourth One-tenth Half One-third One-fourth One-tenth Half One-third 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
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