Structure and Properties of Peptides Disulfide bonds most often stabilize the native structure of intracellular proteins hydrophobic proteins extracellular proteins dimeric proteins intracellular proteins hydrophobic proteins extracellular proteins dimeric proteins ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala, was digested with cyanogen bromide (CNBr) 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 What was the first protein whose complete tertiary structure was determined? Pancreatic DNase Myoglobin Pancreatic ribonuclease Lysozyme Pancreatic DNase Myoglobin Pancreatic ribonuclease Lysozyme ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The oxygen in hemoglobin and myoglobin is bound to lysine residues in the protein histidine residues in the protein the iron atom in the heme group the nitrogen atoms on the heme lysine residues in the protein histidine residues in the protein the iron atom in the heme group the nitrogen atoms on the heme ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Which of the following is an example of tertiary structure in a protein? A P-pleated sheet A multimeric protein A globular domain An a-helix A P-pleated sheet A multimeric protein A globular domain An a-helix ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The oxygen binding curves of hemoglobin and myoglobin are identical are a consequence of the quaternary structure of hemoglobin allow maximum transfer of oxygen to the tissues both (a) and (b) are identical are a consequence of the quaternary structure of hemoglobin allow maximum transfer of oxygen to the tissues both (a) and (b) ANSWER DOWNLOAD EXAMIANS APP
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