3) The following is the amino acid sequence of bradykinin, a peptidereleased by certain organisms in response to wasp stings:Arg – Pro – Pro - Gly – Phe – Ser – Pro – Phe – ArgWhat amino acids or peptides are produced when bradykinin istreated with each of the following reagents?a) with Carboxypeptidase c) with Trypsinb) with Chymotrypsin d) with DNFB

Answered: 3) The following is the amino acid…

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

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This amino acid is: (Note that the non-ionized form is shown; remember that backbone groups are irrelevant to classification) a) Polarized (+) charged b) Nonpolar c) Polar and (-) charged d) Polar uncharged
A peptide composed of 40 amino acids (aa) was isolated from the venom of the Gila Monster(Heloderma suspectum, then submitted to various biochemical and chemical treatments.1) After a treatment with a highly specific chymotrypsin, four peptides were generated:- peptide A (6 aa)- peptide B (16 aa)- peptide C (3 aa)- , and peptide D (15 aa)2) Treatment with carboxypeptidases A or B resulted in the release of:- phenylalanine for peptides A and B- tryptophan for peptide C- glycine for peptide D and the 40 amino acids venom peptide3) One cycle of Edman degradation either for peptide A or for the 40 amino acidspeptide gave the exact PTH derivative indicated below: 4) The 40 amino acids peptide treated with Asp-N endopeptidase followed by massspectrometry MS/MS revealed the following composition:- two molecules of glutamic acid,- various peptides indicated below sorted by masses:HG,DLSKQM,EGTFTS,EAVRLFI,EWLKNGGPSSGAPPPSG Information- Chymotrypsin (endopeptidase) hydrolyzes peptide bonds on…
A peptide was analyzed with the following results. Whatis the primary sequence of the peptide? Briefly state the conclusions of each experimental result and indicate your logic. a)Mass spectrometry was consistent with a peptide of 7 amino acids containing W,C,D,M,N,K, and I. b)One cycle of Edman degradation of the peptide yielded a single product, the PTH derivative of I c)Cleavage of the peptide with CNBr yielded two products. One contained 5 amino acids, and the other 2. One cycle of Edman degradation yielded the PTH derivatives of Iand N, respectively. d)Treatment of the peptide with trypsin yielded 2 products. One of them had significant light absorbance at 280 nm, and Edman degradation yielded the PTH derivative of I. The other trypsin-generated product contained 4 amino acids, and Edman degradation yielded the PTH derivative of Asp.
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-Q-A-P-S-P-L Subjecting this peptide to trypsin would result in OA Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro-Lys Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro-Leu OB. Met-Phe-Val-Trp-Glu-Gin-Arg-Pro-Ser-Pro-Leu OC. D. Met-Phe-Val-Trp-Glu-Gin-Arg and Pro-Ser-Pro-Lys O E. Met-Phe-Val-Trp and Glu-Gin-Arg-Pro-Ser-Pro-Leu
Use the following peptides to answer the questions below: (They are in the image). Which peptide is most negatively charged at pH 7? Which peptide is the most nonpolar? Which peptide contains sulfur? Which peptide will would be most easily detected at 280 nm? Which peptide is the most positively charged at pH 5?
Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.
There is parts A-D for the picture provided. A) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 1? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 B) A peptide has the sequence Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 5? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 C) Same Peptide sequence, What is the net charge at pH8.5, (N-terminus is pronated) Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 D) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 13? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 Thank You!
Imagine that a mutation has been discovered in the HBA1 gene, where amino acid residue # 1 in the alpha subunit is changed from valine to lysine. The structure of these two amino acids is shown below. How would this mutation affect the mobility of HbA in the gel?a) HbA with this mutation would have the same mobility as normal HbAb) HbA with this mutation would have the same mobility as HbSc) HbA with this mutation would have a faster mobility than normal HbA O d) HbA with this mutation would have a mobility somewhere in between HbS and normal HbA
You are analyzing the peptide ala-ile-glu-lys-phe-val- tyr-cys. If you treat the peptide with chymotrypsin, which technique would be best to separate the fragments? O a. ultracentrifugation O b. affinity chromatography O c. dialysis d. gel filtration chromatography O e. ion exchange chromatography What is an advantage of NMR spectroscopy over x-ray crystallography in studying protein structure?
Please answer the following questions 1) based on the structures of adenine, cytosine, guanine, and thyme. Why does A prefer to bind to T and C prefer to bind to G 2) were the binding energies the same for AT and CG? Explain the difference 3) which of the four know bases is the unknown synthetic base most like in terms of its binding characteristics? What does this indicate about its structure? 4) if the unknown synthetic base was used to study DNA replication, which natural bases would it interact with? 5) is the picture question
can u help me
Classify the symmetrical arrangement ofthe subunits (e.g., C2 , C3 , D 2 , helical, icosahedral). 1. Proteobacterial nitrite sensor (3PNS):2. Pseudomonad oligosaccharide receptor (7POR):3. Adenoviral structural protein (8ASP)

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