Hi tutor, can you please solve and teach me how to do this?;1) Find kcat for a reaction in which Vmax is 8 x 10-3 mol/min and the reaction mixture contains two microgram of enzyme (the molecular weight of the enzyme is 100,000 D).;2) An enzyme is considered to have evolved to its most efficient form if;A) kcat is a large number;B) kcat/KM is near the diffusion-controlled limit;C) KM is a large number;D) kcat/KM is a very small number;E) KM is a small number;3) Determine the subunit composition of this protein from the following information;Molecular mass of the native protein by gel filtration is 400 kD;Molecular mass by SDS-PAGE is 200 kD;Molecular mass by SDS-PAGE with 2-mercaptoethanol is 100 kD, 60 kD, and 40 kD;4) Treatment of a short peptide with trypsin gives four fragments with sequences;Leu-Arg;Tyr-Thr-Ser-Val-Trp-Trp-Gly-Lys;Gln-Leu-Phe-Phe-Thr-Leu-Arg;Ala-Asp-Glu-Asn-Lys;Cleavage of the same peptide with chymotrypsin gives six fragments with the sequences;Thr-Leu-Arg-Leu-Arg-Ala-Asp-Glu-Asn-Lys-Tyr;Thr-Ser-Val-Trp;Gln-Leu-Phe;Gly-Lys;Phe;Trp;What is the sequence of the intact peptide?;5) Treatment of a polypeptide with 2-mercaptoethanol yields two polypeptides;(A) Val-Met-Cys-Arg-Gly-Gly-Phe-Arg-Cys-Leu-Ser;(B) Gly-Gln-Asp-Cys-Tyr-Val-Ile-Lys-Glu-Cys-Thr;Treatment with trypsin yields fragments with the following amino acid compositions;Cys2, Glu, Leu, Ser, Thr;Arg, Gly2, Phe;Arg, Asp, Cys2, Gln, Gly, Ile, Lys, Met, Tyr, Val2;Using the two polypeptides above (A and B), indicate the positions of the disulfide bonds in the intact polypeptide.;Analysis of a peptide indicates that there is NO free animo terminal group. Digestion with trypsin yields three peptides with the sequences Ile-Cys-Met-Lys, Asp-Gln-Trp-Asp-Thr-Phe-Lys, and Ser-Gly-Tyr-Arg. Digestion with chymotrypsin yields three peptides with the sequences Arg-Asp-Gln-Trp, Asp-Thr-Phe, Lys-Ile-Cys-Met-Lys-Ser-Gly-Tyr. Draw a diagram of the original peptide.
Paper#17630 | Written in 18-Jul-2015Price : $22