Structure and Properties of Peptides The heme is held in place by a bond between the Fe3+ and histidine the Fe2+ and histidine the Fe3+ and cysteine the Fe2+ and cysteine the Fe3+ and histidine the Fe2+ and histidine the Fe3+ and cysteine the Fe2+ and cysteine ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Disulfide bonds most often stabilize the native structure of intracellular proteins dimeric proteins extracellular proteins hydrophobic proteins intracellular proteins dimeric proteins extracellular proteins hydrophobic proteins ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides In the β-pleated sheet 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 adjacent polypeptide chains can either be parallel or antiparallel ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides In β-pleated sheet structures neighbouring neighboring residues are hydrogen bonded neighboring chains are connected by a-helices chains lie in a flat plane neighboring chains are hydrogen bonded neighboring residues are hydrogen bonded neighboring chains are connected by a-helices chains lie in a flat plane neighboring chains are hydrogen bonded ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides When pO2 = Kd of myoglobin, the fractional saturation (YO2) is about 0.1 1.7 0.9 0.5 0.1 1.7 0.9 0.5 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
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