Answer the following questions based on the structure of the following peptide and the information in the attached table of enzyme activities. M-F-V-W-E-QA-PS-P-L Subjecting this peptide to trypsin would result in OA Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro-Lys 08. Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro-Leu O. Met-Phe-Val-Trp-Glu-Gin-Arg-Pro-Ser-Pro-Leu Met-Phe-Val-Trp-Glu-Gin-Arg and Pro-Ser-Pro-Lys OD. O E. Met-Phe-Val-Trp and Glu-Gin-Arg-Pro-Ser-Pro-Leu

Answer the following questions based on the structure of the following peptide and the information in the attached table of enzyme activities. M-F-V-W-E-QA-PS-P-L Subjecting this peptide to trypsin would result in OA Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro-Lys 08. Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro-Leu O. Met-Phe-Val-Trp-Glu-Gin-Arg-Pro-Ser-Pro-Leu Met-Phe-Val-Trp-Glu-Gin-Arg and Pro-Ser-Pro-Lys OD. O E. Met-Phe-Val-Trp and Glu-Gin-Arg-Pro-Ser-Pro-Leu

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Similar questions

Determine whether each of the amino acids is polar, nonpolar, positively charged, or negatively charged at pH 7. Polar and neutral aspartate H Ser H₂N-C-CH₂-C-COO NH3 lysine Leu Nonpolar Answer Bank H OOC-CH₂-CH₂-C-COO NH3 Positively charged H CH₂-C-COO NH3 hydrophobic amino acids Negatively charged
What step ends the first-half of the chymotrypsin mechanism? Attack of water on the acyl-enzyme intermediate. Selected Collapse of the first tetrahedral intermediate, releasing of the C-terminal peptide fragment and formation of the acyl-enzyme intermediate. Deprotonation of serine by the histidine. Collapse of the second tetrahedral intermediate leading to the final products. REVIEW QUESTION 1/1 CONTINUE MacBook Pro https://virginiacommonwealth.instructure.com/courses/42082/assignments/271397 esc OT
Drag the labels onto the diagram to identify the anatomical terminology describing body orientation and direction (human a Posterior (caudal) Distal Superior (dorsal) Proximal Inferior (caudal) Anterior (ventral) Posterior (dorsal) Pearson arch
Amino Acid 3-Letter 1-Letter Second letter Code Code Alanine Cysteine Aspartic acid or aspartate Glutamic acid or glutamate | Phenylalanine Glycine Histidine Ala Cys Asp Glu UCU Phe UGU cys UGC UUUT UAU Tyr UAC D UUC UC Ser UUA UAA Stop UGA Stop UAG Stop UGG Trp G UCA Phe Leu UUG UCG Gly G H. His Ile CUU CCU CAU CGU U His CAC CÚC Leu CUA CGC CGA Isoleucine Lysine Leucine Pro Arg Lys K CAA Gin CAG CCA Leu L. CUG CCG CG Methionine Met M AUU AUC le ACU) ACC AAU1 AAC AGU Asn Asparagine Proline Glutamine Arginine Serine Asn Ser AGC AGA Arg Pro P. Thr AAA Gln Arg Ser AUA ACA AUG Met ACG AAG Lys AGG R GUU) GCU) GAU1 GGU GGC Gly Threonine Valine Tryptophan Tyrosine Thr GUC Val GUA GCC Ala GCA Val V GAA GAG GGA W Trp Тут Glu GUG GCG GGG Y Apply all that you have learned to solve the following: If you have the following DNA sequence: 5-ATGGCIOTOGTATTAAATAG-3 1. What is the sequence of the bases in the complementary DNA strand in a 3' to 5 direction ?( NB" Just type the letter for the bases) 2.…
Enumerate all the possible DNA nucleotide base sequence for the amino acids given.
A At pH 5, what is the net charge of the peptide Val-His-Gln-Cys-Ser-Lys? 0 -1 0 0+1 Ⓒ +2 Q Search "de 96 5 ******* ******* 131183 J- C 8 a hp
Subjecting this peptide to one cycle of the Edman degradation would result in L-M-F-V-W-E-Q-A-P-S-P Leucine OA. O B. Proline oc Leucine phenylthiohydantoin OD. Proline phenylthiohydantoin None of the above OE.
please identify amino acids in the N terminus in the picture below.
0ミレーNレ NH geometry on both cand N. Torigonal plannes CH - C-N o=), HN CH2 CH-C-OH (a- carbon) CH2 HooC Aspaxagine - Toline - Valine - Arginine - phenylalcmine - Glutamic ocid. 1.Give the name and three letter code for each amino acid in the peptide. e 2. At pH 7, approximately what charge would be on your peptide? Explain your answer. 3. Can your peptide form intra/interchain disulfide bonds? Explain why/why not. e 4. Will your peptide absorb UV and is it fluorescent? Explain why/why not. e 5. What is the probability that your peptide contains a cis peptide bond? Explain your answer.
A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial hydrolysis. From this information, deduce the primary structure of this polypep- tide. Fragments are grouped according to size. Pentapeptide Fragments Tetrapeptide Fragments Phe-Val-Asn-Gln-His Gln-His-Leu-Cys His-Leu-Cys-Gly-Ser His-Leu-Val-Glu Gly-Ser-His-Leu-Val Leu-Val-Glu-Ala
What is the isoelectric point of the following peptide molecule? Asp-His-Glu-Gly-Lys-Tyr-Leu-Phe-Arg-Ser-Cys Relevant pKa values are; 2.2, 3.8, 4.3, 6.0, 8.3, 9.8, 10.1, 10.5, 12.5 and 13.1 3.0 9.1 7.2 5.2 4.1 ONLY one correct answer
please answer part (iii) thank yoh