TABLE 5.1 Properties of the common amino acids found in proteinspKa of lonizing Residue Mass OccurrencepKa ofa-COOH Group a-NH3 GrouppKa ofAbbreviations 1-and 3-letter codesName"Side Chaina(daltons)in Proteins (mol %)AlanineA, Ala2.39.771.088.7ArginineR, Arg2.29.012.5156.205.0.AsparagineN, Asn2.08.8114.114.2Aspartic acidD, Asp2.19.83.9115.095.9CysteineC, Cys1.810.88.3103.141.3GlutamineQ, Gln2.29.1128.143.7Glutamic acidE, Glu2.29.74.2129.126.6GlycineG, Gly2.39.657.067.9|HistidineН, His1.89.26.0137.152.4IsoleucineI, lle2.49.7113.175.5LeucineL, Leu2.49.6113.178.9|LysineK, Lys2.29.010.0128.185.5MethionineМ, Met2.39.2131.212.0PhenylalanineF, Phe1.89.1147.184.0ProlineP, Pro2.010.697.124.7SerineS, Ser2.29.287.085.8T, ThrW, TrpY, TyrThreonine2.610.4101.115.6Tryptophan2.49.4186.211.5Tyrosine2.29.110.1163.183.5ValineV, Val2.39.699.147.2|Approximate valuoc found for gid 4) Using the pk, data found in the supplied chart, determine the predominant charge of each aminoacid at pH 1.0, 6.0 and 12.5Arginine1.06.012.5

Amino acid is amphoteric in nature i.e it can act as both acid as well as . This property is due…

Answered: 4) Using the pK, data found in 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

Enter an estimate for the charge on the peptide KPIVRFDEESC at pH 8.0.
1. What is the possible identity of the AA? a. Aspartic acid b. Lysine c. Alanine d. Proline 2. What is the isoelectric point of AA? 3. What is the pKa responding to the dissociation of the alpha-carboxylic group?
A mixture of five proteins are analyzed by MALDI-TOF. Their molecular weigths are 3 kD, 22 kD, 100 kD, 225 kD and 515 kD. A peak appears in the mass spectrum at 33.3 kD. Which protein most likely gave this peak?
5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=0
1. Sickle cell anemia results from a substitution of a valine for a glutamic acid. What do you expect the effect might be if the mutation were to have placed a leucine at that site? An aspartic acid? 2. Of the following amino acids, glycine, isoleucine, and lysine, which would you expect to be the most soluble in an acidic aqueous solution? Which the least? 3. How many structural isomers could be formed from a molecule with the formula C5H12? C4H8?
A stock solution contains 0.2 mg/mL protein. From this stock solution, 179 uL is diluted with 1.1 mL buffer. What is the concentration of protein in this dilution?
1. Amino Acid 1 = W + X = 1 Draw amino acid 1 at a low pH a) As the D Fisher Projection Name of amino acid 1: b) As the S isomer: Arginine
Are all the proteins separated properly using two-dimensional (2D) gel electrophoresis? Why or why not?
Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.
Which of the following is NOT a unit of concentration? All of these options are units of concentration. mM Moles/Liter Molar You gathered your data from Lab , and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. A 7 fold B 150% C 15 fold D 70%
4)
1) Describe one inner and one outer approach for the prediction of contact or distance maps in proteins.

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

4) Using the pK, data found in the supplied chart, determine the predominant charge of each amino acid at pH 1.0, 6.0 and 12.5 Arginine 1.0 6.0 12.5