Structure and Properties of Peptides Disulfide bonds most often stabilize the native structure of extracellular proteins intracellular proteins hydrophobic proteins dimeric proteins extracellular proteins intracellular proteins hydrophobic proteins dimeric 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 Which hemoglobin chain replaces the beta chain in embryonic hemoglobulin? Delta Gamma Alfa Epsilon Delta Gamma Alfa Epsilon ANSWER DOWNLOAD EXAMIANS APP
Structure and Properties of Peptides Which of the three subunits of the G proteins binds GDP and GTP? Gamma Beta Delta Alpha Gamma Beta Delta Alpha 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
Structure and Properties of Peptides The peptide bond in proteins is usually cis unless proline is the next amino acid usually trans unless proline is the next amino acid only found between proline residues is planar because of steric hinderance usually cis unless proline is the next amino acid usually trans unless proline is the next amino acid only found between proline residues is planar because of steric hinderance ANSWER DOWNLOAD EXAMIANS APP
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