Question 27 QUESTION 27The structure of lysine is shown. Lysine has pk-2.18, pk2-8.95, and pkg-10.53. At pH 9.5, the charge on carboxylic group should be,amino groupand the side chain (Rgroup)- (Record your answer as positive, negative, or zero for each of the blank)H.H.„N-C-cонNH,QUESTION 28Consider the following properties of the listed proteins A, B and C.ProteinplProtein AProtein BProtein CAffinityfor glucoseYesNoNo3.83.87.0Explain clearly how would you physically separte protein B from C in the best and most effective way.(Separation by dialysis, isoelectric focusing and SDS PAGE is NOT an option and cannot be use as answeer choice)For the toolbar,. press ALT+F10 (PC) or ALT+FN+F10 (Mac).BIUSParagraphArial10pt血x X次田田用区Click Save All Answers to save all answers.SaveacerSh StyCourse

Given; pK1= -2.18 pK2=-8.95 pKR=-10.53 at some given pH.

Answered: The structure of lysine is shown.…

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

Question 11. // Hint: Isoelectric focusing separates proteins based on their pI values, and can separate proteins that only differ by a net charge of ±1.±1. Recall that an amino acid residue with a negatively charged R group has a relatively low isoelectric point (pI) where it has zero net charge. Likewise, an amino acid residue with a positively charged R group has a relatively high isoelectric point (pI) where it has zero net charge. Order from Low pH to High pH
Question for protein crystallography- 1. While performing a routine protein crystallization screening, you observe that one of your well drops has doubled in size compared to the remaining wells. Note: the drop in question was set up by taking 1 µL of the protein solution (10 mg/mL LDH in 20 mM TRIS pH 7.5, 0.5 M NaCl and 10% PEG 4000K) and adding it to 1 µL of the crystallization solution (10% PEG 4000K, 50 mM NaCl and 20 mM TRIS pH 8.0). Why did this drop grow larger in size compared to when you initially set it up?
Question:- What is an example of a heterotrimeric G protein and what role does it play?
Question:- The enzyme aromatase is found in the cytoplasm of some cells and converts testosterone to estrogen. You decide to test aromatase from a particular cell, and oops, your lab partner admits he drastically increased the pH in all the test tubes. Which of the following is a likely result? a. The enzyme will be denatured and the substrate will not bind to the active site. b. The enzyme will convert testosterone to estrogen at a faster rate. c. The mistake will have no effect on the experiment, because enzymes are not sensitive to pH. d. The free energy will be lowered and the reaction will not proceed spontaneously.
Text:QUESTION 16 Protein maturation in the ER includes. A Disulfide bond formation B. proteolytic cleavage C attachment of oligosaccharide d. Prolyl isomertzation
Biomaterial question: Give a brief and clear answer, please a. Briefly describe the structural differences between the three major types of biomaterials, including their chemical structure, bonding characteristics, crystal structures, etc. b. Explain briefly the working principle and the information provided by the spectroscopic and chromatographic characterization techniques . Give an example to each of them.
Question: Which base (A, C, T or G) corresponds to X in the unknown? I did the experiment, got the data below, and calculated the binding constants. But I am TOTALLY lost as to how to figure this out! I don't even know what steps I would take. Base pairs Data – all had Temp = 250C PH = 7 Binding Constant A & X [A] = 0.00373221M [X] = 0.00373221M [AX] = 0.0462678M 3.322 C & X [C] = 0.0469007M [X] = 0.0469007M [CX] = 0.00309935M 1.409 T & X [T] = 0.0452279M [X] = 0.0452279M [TX] = 0.00477212M 2.333 G & X [G] = 0.0469554M [X] = 0.0469554M [GX] = 0.00304456M 2.633
Question:- How can we determine trans-membrane domains of proteins in the absence of crystal structure?
Question 4. If you were to synthesize a tetrapeptide consisting of all alanine residues, you would have how many bonds between carbon and nitrogen?
Question:- For a simple enzymatic reaction that involves only one substrate and follows Michaelis–Menten kinetics, the changes in the concentrations of substrate, product, free enzyme, and the enzyme–substrate complex over the course of the reaction are depicted by solid curves in the graph below. Which curve (1 to 4) corresponds to [ES]? Write down the number as your answer.
QUESTION NO. 1Targeting a protein to be degraded within proteasomes usually requires ubiquitin. In the function of ubiquitin all of the following are true except: A. ATP is required for activation of ubiquicin. B. a peptide bond forms between the carboxyl terminal of ubiquitin and an ε-amino group of a lysine . C. linkage of a protein to ubiquitin does not always mark it for degradation. D. the N-terminal amino acid is one determinant of selection for degradation. E. ATP is required by the enzyme that transfers the ubiquitin to the protein to be degraded QUESTION NO. 2Much of procollagen formation occurs in the endoplasmic reticulum and Golgi apparatus which requires signal peptide. All of the following statements about targeting a protein for the ER are true except. A. signal peptide usually has a positively charged N-terminus and a stretch of hydrophobic amino acids. B. signal peptide emerging from a free ribosome binds signal recognition…
Question: A decapeptide composed of ser, ala, IIe. his, trp, phe was treated with 1-flouro- 2,4-dinitrobenzene. It gave a DNP-his on the N terminal and free trp when treated with carboxypeptidase. Upon partial hydrolysis of the peptide, the following fragments were obtained. a. his-lle-phe-ala c. his-ala-phe e. ser-lle-his b. ala-phe-trp d. phe-ala-ser Give the amino acid sequence of the above decapeptide.

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

The structure of lysine is shown. Lysine has pk-2.18. pk2-8.95, and pkg-10.53. At pH 9.5. the charge on carboxylic group should be , amino group and the side chain (R group) -(Record your answer as positive, negative, or zero for each of the blank)