You are studying a novel amino acid. It has an alpha-amino and an alpha-carboxylic group, and anionizable side chain that carries a carboxylic group. A titration curve is shown below.Net chargeaCDf0 1 2 3 4 5+1 [Select]0 [Select]6 7pHChoose the letter that corresponds to the following charges on this novel acid.+2 [Select]-0.5 [ [Select]-1 [Select]8-2 [Select]I9 10 11 12 13

The titration curve of an amino acid shows the change in pH as an acid or base is added to the…

Answered: You are studying a novel amino acid. It…

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

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?
What are the charges of the following amino acids peptides at ph 14? 1. GLAVV 2. RRKKQ
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
This macromolecule is readily available and used extensively.The molecule below is a H H HHH C-H H-C-o HHHH HHHH HHHH H H C-C -C-C H-C-o HHHH H H H H HHH H. H H o-0-H a saturated fatty acid amino acid monounsaturated fatty acid O triglyceride O polyunsaturated fatty acid I-o-z I-O-I I-O-I I-0-I I-O-I I-0-I
Indicate the net charge of cysteine at pH 9.5 Express your answer using two significant figures.
Identify the following types of biomolecules and label and identify all of the functional groups.
From the oligopeptide below, write completely the amino acids and/or peptide fragments that resulted from the reaction of trypsin. The amino acids and residues should be represented by the three-letter abbreviation.
The pka of the side chain of histidine is 6.00. What is the percent of protonated histidine at pH 6.4? 15.3% 28.5% 45.3% O 66.6%
Discuss the reaction conditions you would need to carry out the PEGylation reaction of this peptide and explain how the pH affects the selectivity of these reactions.
Compare the stability of the two salt bridges shown circled in blue at pH 8.4. The carboxylate ions are completely de- protonated at pH 8.4 The pka of the amino group (upper left) is 8.1 and the pka of the amino group (bottom right) is 8.7. (d) NH, F-8- Ed (b) O-H- M5 CH₂COOH (c) 5 (b) CH, CH. H--O=C (d) -H H CH,OH (b) KCHJ NH, (a) The bottom right salt bridge is stronger due to the partial positive charge of +2/3. The bottom right salt bridge is stronger due to the partial positive charge of +1/3. The upper left salt bridge is stronger due to the partial positive charge of +1/3. The upper left salt bridge is stronger due to the partial positive charge of +2/3.
Please be clear in your explanation. I need to figure out how to find the pI of the amino acid. Thank you!
a. what general category would you place this molecule in of the four categories of biomolecules? b. List 5 functional groups you see in this molecule?

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