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 thefragments?O a. ultracentrifugationO b. affinity chromatographyO c. dialysisd. gel filtration chromatographyO e. ion exchange chromatographyWhat is an advantage of NMR spectroscopy over x-raycrystallography in studying protein structure?

Proteins or peptides are a linear chain of amino acids attached together via peptide bonds. Natural…

Answered: You are analyzing the peptide…

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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In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These messages yielded proteinswith the amino acid compositions shown in the followingtable. Using these data, predict the most specific coding compositionfor each amino acid.4/5C:1/5A 4/5A:1/5CPro 63.0% Pro 3.5%His 13.0% His 3.0%Thr 16.0% Thr 16.6%Glu 3.0% Glu 13.0%Asp 3.0% Asp 13.0%Lys 0.5% Lys 50.0% 98.5% 99.1%
There is another melanocyte-stimulating hormone called β-melanotropin.Cleavage of β-melanotropin with trypsin produces the following peptidesplus free aspartic acid. WGSPPK DSGPYK MEHFRIf you assume maximum sequence similarity between α-melanotropin andβ-melanotropin, then what must the sequence of the latter be?
The PAM1 matrix penalizes mismatching amino acids more than higher numbered PAM matrices. Explain why this is true.
A peptide digested with trypsin produced the following three fragments: C, ASFPK, GGRWDGK The same peptide digested with chymotrypsin produced the following three fragments: PKGGRW, DGKC, and ASF What is the primary structure of the peptide?
In the laboratory a team of peptide/protein chemists synthesize the HIV-1 protease from all D-containing amino acids. Answer the following questions related to this synthetic HIV-1 protease. The HIV-1 protease would DA cut polypeptides with a certain sequence if they are made of D-amino acids. OR assume a tertiary structure that is the mirror image of the normal HIV-1 protease. nc cut polypeptides with a certain sequence if they are made of L-amino acids. OD process the proteins expressed on infection by the natural HIV-1 pathogen. DE behave exactly like the normal HIV-1 protease. tinn will save this response. Question 34 of 55
Refer to the sequence below to answer the following questions. 5’- CACTTTTCAACTTGGCAGAAGCAATGTATCTCCGGATATAATCGCTTTCGAATTCG- 3’ 3’- GTGAAAAGTTGAACCGTCTTCGTTACATAGAGGCCTATATTAGCGAAACTTAAGC- 5’ Is the sequence from a bacterial or a eukaryotic cell?Identify the characteristics that support the rationale for your decision. Which DNA strand serves as the template for transcription?
Reverse translate the sequence of insulin pasted below:MALWMRLLPLLALLALWGPDPAAAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCNUse the webserver listed here:https://www.ebi.ac.uk/Tools/st/emboss_backtranseq/Please optimize the codons for Homo sapiens or Escherichia coli. Are the DNA sequences different?
What are the Okazaki fragments?
Give typing answer with explanation and conclusion The following gene codes for a liver enzyme. Changing the A/T base pair to which of the following would result in a missense mutation? 5’ GCCTAATATGCCCGTATGC(AGC)nCGAATAAAATAGTACGGTCGTCGC 3’ 3’ CGGATTATACGGGCATACG(TCG)nGCTTATTTT ATCATGCCAGCAGCG5’ A. C/G B. T/A C. G/C D. Any of the above E. 2 of the above F. None of the above
What is the purpose of Southern's blotting technique? Explain in detail the biochemical principle that underpin each step of the method.
I. A protein, X, was Isolated from a pathogenlc mlcroorganism. The proteln Is a vlrulence factor whose path0genlclty lies In a heptapeptide of unknown sequence. After trypsin cleavage of the heptapeptide from protein X, the peptlde's compOsition and sequence was determined. The fOllowing were the results of the sequenclng process: 1. When the peptide was treated with dinitrofluorobenzene (DNFB), DNP-asp and a mixture of amino acids were produced. 2. When the same Intact peptide was treated with streptococcal protease, a pentapeptide of composition asp, asN, cys, gly and ser and 2 amlno acids were released. 3. When the heptapeptlde was also treated with hydrOxylamine HCI, a tripeptide and a tetrapeptide were obtained. The C-terminal amino acid of the tripeptide was asN. 1) What is the sequence of the heptapeptide if it is composed of cys, asp, lys, asN, gly and ser only? 2) What is the pl of the heptapeptide?
how would you identify whether or not complete resolution of the three amino acids has been achieved

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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