answer both please The peptide below is placed into a buffer with a pH = 6.65HN-CH-ČH3NH--CH-NH-CH-C-NH-CH--NH-CH-CонCH2CH2CH2HN-C=NH,NH2CH2CHH3CCH3HO-CH,онWhat direction will the peptide move?If it will move towards the positive electrode give your answer as 1If it will move towards the negative electrode give your answer as -1If it will not move give your answer as 0 The peptide belowHạN-CH--NHCHNH-CH-CNH-CH-CNH-CH-O-CH2CH2CH2CH2OHCH2ноCH2CH3HNc=NH;NH2needs to be separated from a second peptide with a primary sequence ADES.At what pH range would it be possible to separate the peptides?9.0-11.0O 7.4O 0-2.0O 12.0-14.0

An amino acid's zwitterion exists at pH = isoelectric point. Each amino acid has a unique pI value…

Answered: The peptide below is placed into a…

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

A peptide in a solution with a pH of 7 has the following sequence: K-R-E-D-H-D-E (Lys-Arg-Glu-Asp-His-Asp-Glu). To get to the pI, you would need elevate the pH.
A peptide in a solution with a pH of 7 has the following sequence: K-R-E-D-H-D-E (Lys-Arg-Glu-Asp-His-Asp-Glu). To get to the pI, you would need elevate the pH. True or False
Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show them in zig-zag style, from amino to carboxy terminus, with correct stereochemistry Draw the predominant form at pH = 2 Draw the predominant form at pH = 5 Draw the predominant form at pH = 7 Draw the predominant form at pH = 12
Please help! Sketch a titration curve of the peptide Ala-Tyr-Gln-Met-Asp-His from pH=0 to 14 up to 5 equivalnets of KOH (Please type answer)
A peptide with 12 amino acids has the composition (not sequence) Asp 2Cys 2Glu 2Leu 2Ser 2Tyr Val. It also has Ser as the N-terminal residue and Cys as C-terminal. Partial acid hydrolysis gave these peptide sequences: (a) SerLeuTyr (b) TyrCys (c) LeuTyrGlu (d) GluLeuGlu (e) SerValCys (f) CysSerVal (g) GluAspTyr . What is the peptide sequence?
The sequence of a 29 aa long peptide can be determined from the following data: Treatment of the peptide with dansyl chloride reveals that the amino-terminal is Val. Trypsin digestion, separation of peptides, and Edmann technique give the sequences for peptide fragments as follows: T-1 V-G-A-H-A-G-E-Y-G-A-E-A-T-E T-2 A-A-W-G-KT-3 V-L-S-P-A-K T-4 T-N-V-K
Which peptide has a larger pI? Arg-Gly-Gly-Gly or Gly-Gly-Gly-Arg why?
PEPTIDE #1: Pro-Phe-Thr-Cys PEPTIDE #2: Gly-Tyr-Ser-Asp Calculate the pI of both peptides. Which is more acidic and why? Which one is more hydrophobic? Which peptide sequence (#1 or #2) would be more likely situated on the surface of the protein?
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...
Using proper convention, provide the amino acid sequence for the following peptide.
Remembering that the amino acid side chains projecting from each polypeptide backbone in a β sheet point alternately above and below the plane of the sheet, consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg- Leu-Lys-Ile-Arg-Phe-Glu. Do you find anything remarkable about the arrangement of the amino acids in this sequence when incorporated into a β sheet? Can you make any predictions as to how the β sheet might be arranged in a protein?
Draw the structure of peptide with the following amino acids Gly-Leu-Ala-Gly-Pro-Hyp. The structure formed of the peptide is most likely a? Please explain. Thank you!

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