H-Bond donors PSA 1532 55 140 60 75 Which of the following compounds is more likely to be a substrate for Pgp: Compound H-Bond acceptors MW Ionization A 350 pKa=3 B 520 pKa=9 CD 400 pKa=4 D 470 pKa=8 4038
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- What is the difference between an enol phosphate and a normal phosphate ester that gives PEP such a high phosphoryl group transfer potential?What sidechain residues stabilize binding of PSTMB in the LDHA structure? https://www.nature.com/articles/s41598-019-40617-3An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.
- The amln0 acid histldine ls usually found in actlve sltes 0f enzymes. What structural feature does the R group of hlstidine have that may be important for the activity of enzymes? ExplainLooking at the structure of RDV-TP, what changes in the structure of the molecule does the active form of Remdesivir have that the naturally occurring ATP does not have. a) Amine group, NH2, on position 6 of purineIn many biochemical reactions which involves the formation of an enolate intermediate, the carbonyl oxygen of the substrate is coordinated to a divalent metal ion (usually zinc or magnesium) in the active site. Explain with structural drawings, how this ion-dipole interactions affect the acidity of the a-protons?
- AH = - 1.2 kcal/mol; Кр 3 16 nM OH 1 HO AH = - 6.0 kcal/mol; Kp = 76 nM OH HOll AH = - 5.5 kcal/mol; Kp = 0.5 nM OH 3 (iv) Consider the molecule 1 being derivatized to yield molecule 2. How would you expect AG for the binding process (to their target) of 2 to compare to 1? Justify your answer.What is the catalytic triad of chymotrypsin? Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytic triad and the significance of the oxyanion hole.Draw the structure of pentapeptide Trp-Asp-Cys-Lys-Gln that would predominate in aqueous solution at pH=5.5. (Relevant pKa values are 2.2, 3.8, 8.3, 9.6 and 10.5.)
- Determine the net charge on the following pentapeptide "Lys-Ala-His-Asp-Ser" at: a. pH 1.0 b. pH 10.1Draw the structure of the PTH derivative product you would obtain by Edman degradation of the following peptides: (a) I-L-P-F (b) D-T-S-G-ADraw the first tetrahedral intermediate of the chymotrypsin mechanism (a single structure, no arrows required). Circle the oxyanion hole. How does the oxyanion hole of chymotrypsin compare to that of carboxypeptidase?