Structure and Properties of Peptides The major element of secondary structure in myoglobin and hemoglobin is All of these the a-helix the reverse turn the P-strand All of these the a-helix the reverse turn the P-strand ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The nature of peptide bond can be best explained as partial double bond truly double bond Hydrogen bond Van der waals force partial double bond truly double bond Hydrogen bond Van der waals force ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The oxygen binding curves of hemoglobin and myoglobin 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) are identical are a consequence of the quaternary structure of hemoglobin allow maximum transfer of oxygen to the tissues 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 The different orders of protein structure are determined by all of the following bond types except phospho-diester bonds disulfide bridges hydrogen bonds peptide bonds phospho-diester bonds disulfide bridges hydrogen bonds peptide bonds ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Hydrogen bonds in a-helices are not present at Phe residues analogous to the steps in a spiral staircase more numerous than Vander Waals interactions roughly parallel to the helix axis not present at Phe residues analogous to the steps in a spiral staircase more numerous than Vander Waals interactions roughly parallel to the helix axis ANSWER DOWNLOAD EXAMIANS APP