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 Heme is the binding pocket of myoglobin and hemoglobin and is composed of polar residues negatively charged residues hydrophobic residues positively charged residues polar residues negatively charged residues hydrophobic residues positively charged residues ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Peptides in the fully extended chain conformation 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 do not occur in nature also have a cis geometry in their peptide bonds have Y = F = 180° ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides When pO2 = Kd of myoglobin, the fractional saturation (YO2) is about 1.7 0.1 0.9 0.5 1.7 0.1 0.9 0.5 ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides In the β-pleated sheet 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 the polypeptide chain is fully extended adjacent polypeptide chains can either be parallel or antiparallel hydrogen bonds are formed between the peptide bonds ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides The same peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala. was digested with chymotrypsin 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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