Question 2 1 pts Given the following peptide: Leu-Arg-Asp-Phe-Al...

Question 2 1 pts Given the following peptide: Leu-Arg-Asp-Phe-Ala-Lys-Met-Thr What would be the resulting peptides or amino acid when it is cleaved with Chymotrypsin Leu-Arg-Asp-Phe-Ala-Lys-Met and Thr Leu-Arg; Asp-Phe-Ala and Lys-Met-Thr no cleavage will occur Leu-Arg-Asp-Phe and Ala-Lys-Met-Thr Leu-Arg-Asp-Phe-Ala and Lys-Met-Thr Question 3 1 pts Which of the following correctly describes "salting out"? Salts compete with proteins for interactions with water which increases the solubility of the protein Salts form ion-dipole interactions with the protein which decreases the solubility of the protein Salts form ion-dipole interactions with the protein which increases the solubility of the protein Salts compete with proteins for interactions with water which decreases the solubility of the protein Question 5 1 pts What effect is seen on a Lineweaver-Burke graph when a competitive inhibitor is added to an enzymatic reaction? both the y-intercept and the slope change the line is inversed the y-intercepts changes the slope of the line changes neither the y-intercept nor the slope change Question 7 1 pts Considering enzyme mechanisms, what group is often attacked by a nucleophile? The nitrogen atom of the imidazole group. The carbon atom of a carbonyl group. The oxygen atom of an alcohol group. The 3'-hydroxyl group of nucleosides and nucleotides. The R-group of leucine. Question 9 1 pts Chymotrypsin does not work well at pH 4 because: His57 cannot work as general base Ser195 cannot work as nucleophile His57 cannot work as general acid The oxyanion would extract protons