Structure and Properties of Peptides The major element of secondary structure in myoglobin and hemoglobin is the a-helix the reverse turn the P-strand All of these the a-helix the reverse turn the P-strand All of these 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 polar residues positively charged residues negatively charged residues hydrophobic residues polar residues positively charged residues ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The oxygen in hemoglobin and myoglobin is bound to histidine residues in the protein lysine residues in the protein the nitrogen atoms on the heme the iron atom in the heme group histidine residues in the protein lysine residues in the protein the nitrogen atoms on the heme the iron atom in the heme group ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The peptide bond in proteins is usually trans unless proline is the next amino acid only found between proline residues is planar because of steric hinderance usually cis unless proline is the next amino acid usually trans unless proline is the next amino acid only found between proline residues is planar because of steric hinderance usually cis unless proline is the next amino acid ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Which of the following is an example of tertiary structure in a protein? A globular domain A P-pleated sheet A multimeric protein An a-helix A globular domain A P-pleated sheet A multimeric protein An a-helix ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Peptides in the fully extended chain conformation do not occur in nature also have a cis geometry in their peptide bonds have Y = F = 180° are equivalent to the (3-sheet structure do not occur in nature also have a cis geometry in their peptide bonds have Y = F = 180° are equivalent to the (3-sheet structure ANSWER DOWNLOAD EXAMIANS APP
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