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 In the β-pleated sheet the polypeptide chain is fully extended adjacent polypeptide chains can either be parallel or antiparallel hydrogen bonds are formed between the peptide bonds All of these the polypeptide chain is fully extended adjacent polypeptide chains can either be parallel or antiparallel hydrogen bonds are formed between the peptide bonds All of these ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Peptides in the fully extended chain conformation do not occur in nature have Y = F = 180° are equivalent to the (3-sheet structure also have a cis geometry in their peptide bonds do not occur in nature have Y = F = 180° are equivalent to the (3-sheet structure also have a cis geometry in their peptide bonds ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The major element of secondary structure in myoglobin and hemoglobin is the P-strand the reverse turn the a-helix All of these the P-strand the reverse turn the a-helix All of these ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides What was the first protein whose complete tertiary structure was determined? Myoglobin Pancreatic DNase Lysozyme Pancreatic ribonuclease Myoglobin Pancreatic DNase Lysozyme Pancreatic ribonuclease ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides What is the effect of a decrease in pH on hemoglobin oxygen affinity? Increase in oxygen affinity No effect on oxygen affinity Increase affinity in muscle cell otherwise decrease Decrease in oxygen affinity Increase in oxygen affinity No effect on oxygen affinity Increase affinity in muscle cell otherwise decrease Decrease in oxygen affinity ANSWER DOWNLOAD EXAMIANS APP
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