Consider the hypothetical serine protease in the image, which shows the specificity pockets. The S1 pocket has a glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S1' pocket is deep and hydrophobic. R3 Suggest a 3-amino acid sequence that this protease would cleave and indicate between which sites the peptide bond R would be broken. S2 Which sequence would this protease cleave? O Leu-Val-Arg Arg-Val-Leu Val-Leu-Arg Val-Arg-Leu Leu-Arg-Val Arg-Leu-Val

Consider the hypothetical serine protease in the image, which shows the specificity pockets. The S1 pocket has a glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S1' pocket is deep and hydrophobic. R3 Suggest a 3-amino acid sequence that this protease would cleave and indicate between which sites the peptide bond R would be broken. S2 Which sequence would this protease cleave? O Leu-Val-Arg Arg-Val-Leu Val-Leu-Arg Val-Arg-Leu Leu-Arg-Val Arg-Leu-Val

Biochemistry

9th Edition

ISBN:9781305961135

Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Chapter3: Amino Acids And Peptides

Section: Chapter Questions

Problem 10RE: MATHEMATICAL Calculate the isoelectric point of each of the following amino acids: glutamic acid,...

See similar textbooks

Similar questions

Need help The β chains of HbA and HbS were treated with trypsin, and the sequence of the N-terminal tryptic peptides are as given below. Do these peptides separate from each other in an electric field if the pH is 7.0? Explain in detail the reasoning behind your answer and include your calculations for the charge of each peptide in your answer. HbA: Val-His-Leu-Thr-Pro-Glu-Glu-Lys HbS: Val-His-Leu-Thr
wnich snows tne specinicity pockets. The S pocket nas a Ra glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S,' pocket is deep and hydrophobic. Suggest a 3-amino acid sequence that this protease would R2 H cleave and indicate between which sites the peptide bond would be broken. S2 Which sequence would this protease cleave? Val-Lys-Phe Phe-Lys-Val Lys-Phe-Val Val-Phe-Lys Phe-Val-Lys O Lys-Val-Phe The peptide bond that is broken is between which sites? O S2 and S,' OS, and S,' O S2 and S1 O S2 and S1, and S and S,' IZ
Please help! Sketch a titration curve of the peptide Ala-Tyr-Gln-Met-Asp-His from pH=0 to 14 up to 5 equivalnets of KOH (Please type answer)
GT 3 A. Write the structure of the pentapeptide GLDSC. B. What is the complete name of this pentapeptide? Show a tertiary structure of ACGGC after a disulfide bond forms. A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin; the other was treated with cyanogen bromide. Given the following sequences (N-terminal to C- terminal) of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment Asn-Thr-Trp-Met-lle-Lys Gly-Tyr-Met-Gln-Phe Val-Leu-Gly-Met-Ser-Arg Cyanogen bromide treatment Gln-Phe Val-Leu-Gly-Met lle-Lys-Gly-Tyr-Met Ser-Arg-Asn-Thr-Trp-Met
GT 3 A. Write the structure of the pentapeptide GLDSC. B. What is the complete name of this pentapeptide? 1. Show a tertiary structure of ACGGC after a disulfide bond forms. A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin; the other was treated with cyanogen bromide. Given the following sequences (N-terminal to C-terminal) of the resulting fragments, deduce the sequence of the original peptide. 2. 3. Trypsin treatment Asn-Thr-Trp-Met-lle-Lys Gly-Tyr-Met-GIn-Phe Val-Leu-Gly-Met-Ser-Arg Cyanogen bromide treatment Gln-Phe Val-Leu-Gly-Met lle-Lys-Gly-Tyr-Met Ser-Arg-Asn-Thr-Trp-Met
need help to calculate P1 for amino acid Tryptophan. Also please check if I draw the mechanism correctly and completely？？？
Part C - Exploring antiparallel 3 sheet structure The hydrogen bonding between antiparallel sheets, also visible in the pdb by selecting the antiparallel sheet view, is shown. Locate the N- and C-termini in this image. Select the antiparallel sheet view in the pdb file. How many peptide chains are shown? O 1 O 2 3 O 4 Submit Request Answer
MATHEMATICAL Calculate the isoelectric point of each of the following amino acids: glutamic acid, serine, histidine, lysine, tyro- sine, and arginine.
MATHEMATICAL The hydrolysis of a phenylalanine-containing peptide is catalyzed by -chymotrypsin with the following results. Calculate KM and Vmax for the reaction. PeptideConcentration(M)Velocity(Mmin1)2.51045.010410.010415.01042.21065.81065.91067.1106
Problem: From the following information determine the amino acid sequence of a peptide. N-terminal Edman gives PTH-Alanine C terminal carboxypeptidase treatment, no observable reaction Trypsin cleavage gives three products Arg Peptide containing Ala, Lys Peptide containing Asp, Met, Phe, Pro Mild Chymotrypsin cleavage gives 2 peptides Peptide containing Asp, Pro Peptide containing Ala, Arg, Lys, Met, Phe CNBr cleavage gives 2 peptides Peptide containing Ala, Arg, Lys and homoserine Peptide containing Asp, Phe, Pro You must supply the answer as the 3-letter amino acid sequence from N-terminus to C-terminus in the form (you must use dashes, not spaces between the amino acids) Met-Thr-Glu-Trp
Problem: From the following information determine the amino acid sequence of a peptide. N-terminal Edman gives PTH-Alanine C terminal carboxypeptidase treatment, no observable reaction Trypsin cleavage gives three products Arg Peptide containing Ala, Lys Peptide containing Asp, Met, Phe, Pro Mild Chymotrypsin cleavage gives 2 peptides Peptide containing Asp, Pro Peptide containing Ala, Arg, Lys, Met, Phe CNBr cleavage gives 2 peptide Peptide containing Ala, Arg, Lys and homoserine Peptide containing Asp, Phe, Pro You must supply the answer as the 3-letter amino acid sequence from N-terminus to C-terminus in the form (you must use dashes, not spaces between the amino acids)
C- PETT-1 PETT-2 It seems PETT-2 worked better than PETT-1. Examine each structure carefully. Provide plausible reasons for the differences in these compounds inhibiting their target enzyme, reverse transcriptase. How might you improve the efficacy of PETT-1 and PETT-2?