At which pH would the peptide with the amino acid sequence 'KEYHR' be found in anIPG (Immobilized pH gradient) strip after successful isoelectric focusing. Showcalculation.lonizable groupsAlpha amine group of KSide chain group of KSide chain group of ESide chain group of YSide chain group of HSide chain group of RAlpha carboxylic acid group of Rpka8.9510.534.2510.07612.482.17

Recall that:A peptide is a short chain of amino acid residues linked together via a peptide bond.…

Answered: At which pH would the peptide with 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

See similar textbooks

Similar questions

An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.
the following peptide is incubated as chymotrypsin: Gly-Val-Phe-Lys-Ala. Present the detailed chemical mechanism by which chymotrypsin hydrolyzes this peptide. Briefly explain each step. Include only the structure of the final products of the reaction.
Identify the a-carbon of aminolevulinic acid.
The melanocyte-stimulating peptide hormone a-melanotropin has the following sequence:Ser–Tyr–Ser–Met–Glu–His–Phe–Arg–Trp–Gly–Lys–Pro–Val(a) Write the sequence using the one-letter abbreviations.(b) Calculate the molecular weight of a-melanotropin, using data inTable
The pH vs charge graph for a triprotic amino acid is shown below. Please answer the following questions about the amino acid. Net Charge 0 2 4 Alpha amino [Select] 6 R [Select] pH a. Which of the following triprotic amino acids is this? Alpha carboxyl [Select] 8 10 12 [ Select] 14 1 0.5 0 -0.5 -1 b. What is the isoelectric point? (Please select the appropriate range in which the isoelectric point falls) (Hint - look up the pKa values in the pKa table for amino acids, which was in video one of today's lecture) [Select] -1.5 c. What form of this amino acid dominates at a pH of 14? Please select the correct form for each ionizable group. -2
Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Myoglobin 7.0 16.7 What is the appearance after visualization of a protein mixture containing the seven proteins above if 2D gel electrophoresis is done?
The ideal buffer range for any amino acids is pH above or below its pI values because the amino acid will get get precipitated at its pI. pKa1 of -COOH group of Cys = 1.71 pKa2 of -NH2 group of Cys = 10.78 pKa3 of side chain group of Cys = 8.33 (it indicates that the thiol group of Cys is a strong acid than the -NH2 group pf Cys as pKa Cys side chain is lower). Thiol side chain of Cys will loose proton first than -NH2. Net charge on Cys is zero in structure B, i.e. Structure B is a zwitterion and pI can be calculated from pKa1 and pKa3. Structure B of Cys, pI = (8.33 + 1.71) / 2 = 10.04/2 = 5.02 pH above its pI the Cys will be -vely charged (deprotonated) while pH below its pI it will be +vely charged (protonated). So, selection of buffer depends on its pI values, not pKa values of each functional group, QUESTION: What are the buffer regions/effective pH range?
Consider a protein in which a negatively charged glutamic acid side chain (pKa=4.2) makes a salt bridge (ion-ion interaction) with a positively charged histidine side chain (pKa=6.5). Part C: Justify your answer with calculations of partial charges on these amino acid side chains at pH=7.9.(Hint: Consider lessons from Coulomb's law, and the Henderson-Hasselbalch equation.)
What are the charges of the following amino acids peptides at ph 14? 1. GLAVV 2. RRKKQ
Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Мyoglobin 7.0 16.7 What is the appearance after visualization of a protein mixture containing the seven proteins above when subjected to SDS-PAGE?
draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 and put each charges beside the amino acids then compute for the isoelectric point please show complete solution KRINPLA
Regarding to ALL the 20 standard amino acids1. Are ALL the 20 standard amino acids asymmetric and chiral molecules?2. Do they contain the elements C,H,N,O,S3. do they have high boiling oils at room temperature

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS