The sequence of a peptide is given below.YGGFMTSEKSQTPLVTLFKNAIIKNAYKKGEIf you perform peptide sequencing by tandem mass spectroscopy, calculate the predicted m/z ratio for b1,b5, b12, y1, y5 and y12 ions.

Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

Answered: The sequence of a peptide is given…

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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Similar questions

Compare and contrast the following protein characterization techniques in terms of the principles governing their functions. affinity chomotagraphy vs hydrophobic interaction chromatography
Using mass spec, the primary structure of 4 peptides is obtained from a tissue sample: VMDEL, GHKRT, CNPQI, and SAWFY. The pI of each peptide is calculated and ion exchange chromatography is used to purify each peptide. VMDEL, GHKRT, CNPQI, and SAWFY were separated into 4 pure samples. The labels on all the samples are erased by mistake, and the mass spec is no longer working. You can run a few simple tests to identify the samples. What are 4 tests to identify each peptide and why?
You were able to extract an amino acid sequence from an unknown protein you process through mass spectrophotometry. How will you able to identify the said protein and its function?
How can a mass spectrometer be used to identify the protein/s excised from a 2D gel?
Which method of chromatography would be the most appropriate for separating mixtures of thefollowing peptides at a neutral pH? (a) ARDDEKLLML, LMYWWILLDETSARALIV, DQNNA(b) GATSKKIVLM, ASCILLVMEN, MFDDAAYVNE(c) KLMDAATSPFLMAGHHHHHH, MFPSATEKRQQNNESTVLAG In what order would the following peptides be eluted from an anion exchange column at pH 7.5?Peptide 1: Ala–Asp–Glu–Gln–Trp–Leu–His–ValPeptide 3: Phe–Gln–Glu–Ala–Gln–His–Leu–Arg-IlePeptide 2: Arg–Ile–Pro–Lys–Cys–Met–Lys
Compare and contrast the following protein characterization techniques in terms of the principles governing their functions. size exclusion chromatography vs ion-exchange chromatography
Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Gly-Phe-Met-Cys- which of the following test will the sample be positive? Lead-sulfide test Hopkins cole's test Millon's test Xanthoproteic test
Compare and contrast the following protein characterization techniques in terms of the principles governing their functions. electrosrapy ionization mass spectrometry vs polyacrylamide gel electrophoresis
Please draw the given peptide and calculate the net charge at pH 1, 4, 8 and 12. GRNVGHEWA
You assay 0.5 ml of 1/2000 diluted egg white for protein, as described in the practical schedule, and the spectrophotometer reading at 595 nm is 0.6. Using the attached calibration curve(click to enlarge), calculate the concentration of protein in undiluted egg white. Give your answer in mg/ml.
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When pure hemoglobin (molecular mass of 64,000 Da) is separated by the following methods, what major molecular mass species do you expect to see? Gel filtration chromotography: Gel filtration with 6M Urea: SDS-PAGE with DDT: SDS-PAGE:

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The sequence of a peptide is given below. YGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE If you perform peptide sequencing by tandem mass spectroscopy, calculate the predicted m/z ratio for b1, b5, b12, y1, y5 and y12 ions.