ChemistryPLEASE #6. Question 6At pH 9.0, which of the peptides listed in Question #4 would bind tightest to a hydrophobic interaction chromatography column?O Peptide IO Peptide IIO Peptide III 0Question 4A mixture of three peptides is provided to you to separate. The sequences of the three peptides are known:1. KMWRR (pl = 12.01)II. DHEIE (pl = 4.13)III. YWIFW (pl= 5.52)Assuming the concentration of all three peptides in the mixture is equal,Which of the three peptides will have the least absorbance at 280 nm? Peptide IlWhich of the three peptides will have the greatest absorbance at 280 nm? Peptide III

Hydrophobic interaction chromatography (HIC) separates molecules based on their hydrophobicity. HIC…

Answered: Question 6 At pH 9.0, which of the…

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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"Regarding resolution of mass spectrometers and various ways mass of peptides can be represented, which is or are true? " "A larger peptides will have a smaller difference between the monoisotopic and average masses, compared to smaller peptides, because the contribution of 13C is greater. " Higher resolution allows investigators to distinguish between monoisotopic masses and other masses of otherwise identical peptides. "Average mass size is always smaller than monoisotopic mass, because 13C and 15N contribute to monoisotopic mass. " "Monoisotopic mass is calculated as if there are no heavy isotopes within the peptide, and so is always smaller than the average observed mass."
Draw the structure of peptides TGPNLHGLFGR and ELAGAPPEPA, and calculate m/z values of their an, bn, and yn sequence ions.
Hydrogen bonds are usually 2.7-3.3 angstrom long. According to this information, do you think there is a direct hydrogen bonding between H840 and the phosphodiester bond that links dG13 and dT14 (Chain C)? If not, what is the key role of H840 in Cas9?
Take a look at the multiple-sequence alignment shown ofthe globin polypeptides, focusing on amino acids 101 to 148.A. Which of these amino acids are likely to be most important forglobin structure and function? Explain why.B. Which are likely to be least important?
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
Sir Bong wanted to determine the a amino acide sequence og BONG. The summary of the analyses performed to the peptide is attached. 1. The three letter designation for the N terminal amino acid residue of CUTE is? 2. The three letter designation for the N terminal amino acid residue of POGI is? 3.The three letter designation for the N terminal amino acid residue of BONG is? 4. The ONE letter designation for the N terminal amino acid residue of CUTE is? 5. The ONE letter designation for the N terminal amino acid residue of POGI is? 6. The ONE letter designation for the N terminal amino acid residue of BONG is? 7.The ONE letter designations for the fragments produced upon treatment of POGI with chymotrypsin are? 8. The ONE letter designations for the fragments produced upon treatment of BONG with thermolysin are?
1. Which peptide would be more soluble at pH 7.0, (Val)₂₀ or (Asp)₂₀ ? at pH 3.0, (Gly-Glu-Val)
1CFD CALCIUM-FREE CALMODULIN How long is the protein’s primary sequence?Does this protein have any secondary, tertiary and/or quaternary structures present?Are there any molecular additions to this protein that are not amino ac
1a) In MALDI-TOF data, when performing peptide mass mapping search, the number of peptides and the sequence coverage decreases, but protien score increase. Explain b) As the same as part a, the peptide masses and the coverage remain the same, but the protien score increase, explain how this can happen.
You are trying to determine the PTMs on your protein of interest, so you set up a mass spectrometry experiment. You get the following data. Starting sequence: PRTEINSKICKASSDER After Trypsin digest, you get the following major peptides and weights from MS: TEINSKICK/1167 Da ASSDER/664 Da a. Which of these peptides is modified? b. What is the modification?
Chymotrypsin digestion, separation of peptides, and Edmann technique give the sequences for peptide fragments as follows: C-1 G-A-E-A-T-E C-2 G-K-V-G-A-H-A-G-E-Y C-3 V-L-S-P-A-K-T-N-V-K-A-A-W What is the sequence for the peptide? NOTE: Label the fragments when reconstructing the peptide chain e.g. for trypsin T-1, T-2 etc...
Please calculate and plot the charge on a peptide with the sequence of NEYK over the pH range from 1 to 13. Please use the pKa values from the table. You may calculate the charge at 1 pH unit intervals.

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Question 6 At pH 9.0, which of the peptides listed in Question #4 would bind tightest to a hydrophobic interaction chromatography column? O Peptide I O Peptide II O Peptide III