Which of the following compounds is most similar to the transition state of peptide bondhydrolysis?A.R2D.R2-HHO.R1Nمیں ملیB.R2مل ما-R1E.OHR2C-R1

"peptide hydrolysis" is defined as the breaking of peptide bind by adding water molecule to the…

Answered: Which of the following compounds is…

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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Which of the following is incorrect about the peptide Arg-Asp-Cys-Tyr-Gln-Arg-Glu? O a. Its estimated MW is 770 Da b. None; all the other choices are correct OC. At pH 7, it has a net charge of zero O d. At pH 7, it has six charged groups
The amino acid shown below has an ionizable side chain with a pka of 4. When this amino acid is in a more basic solution (i.e., pH 11), it would resemble ionization state C and have a charge of -1 HO OH NH₂ lonization state A NH3 lonization state C HO OH NH3+ Ionization state B dyb NH₂ lonization state D
Which of these amino acids is a hydrophobic amino acid? (Select all that apply, if necessary.) A. B. C. D. E. iº H₂N-CH-C CH₂ T CH₂ CH₂ NH C=NH2 NH₂ amino acid E amino acid D amino acid B amino acid C amino acid A 200 H₂N-CH-C CH₂ C=O I OO H₂N-CH-C- CH₂ CH₂ T C=O T NH₂ 0 H₂N-CH- CH₂ CH-CH3 CH3 H₂N-CH-C CH₂ I OH -0
Two peptide sequences are shown below.Peptide A: N-term – GDL – C-termPeptide B: N-term – GTL – C-terma. Draw each peptide at physiological pH. Circle each ionizable functional group in your drawing.b. Briefly explain why changing aspartate to threonine changes the number of ionizable functionalgroups in the peptide chain.c. Briefly explain why the functional group found in aspartate’s side chain is ionizable but the functionalgroup found in threonine’s side chain is not.
The tripeptide +H3N-Leu-His-Glu-COO- has pKa values of 2.2, 3.6, 6.0 and 9.1. The isoelectric point (pI) for this peptide will be: 8 5 6 4 None of the above
The structure of a peptide is shown below: OH HN NH, How many hydrolytic products will be obtained by cleavage with trypsin, a protease? А. 2 В. 3 О С.4 O D. 5 E. none; trypsin will not cleave the peptide
Consider the tripeptide phenylalanylcysteyl methionine. Part: 0 / 2 Part 1 of 2 Draw the structure of this tripeptide at physiological pH. Click and drag to start drawing a structure. : ☐
Draw the structural formulas of the following peptides, andshow which bond would be cleaved by chymotrypsin.a. trp-val-glyb. phe-ala-pro
Which of the following statements concerning the peptide NH3*-Val-Ala-Gly-Lys-Leu-Gly-Val-Phe- Tyr-lle-COOH is correct? O The peptide can form an alpha-helical secondary structure O The peptide can form a beta-pleated sheet O The last amino acid residue is Val. O Three peptide linkages are present.
Match the chemical properties with the amino acid (note: the charges are not indicated on the charged amino acids) A. NH3+ - CH - COO- I (CH)2 I OH N,N - DimethyltryptamineAspartic acid B. NH3+ - CH - COO- I (CH)4 I NH2 Which one of each of these is: uncharged and polar charged and non-polar negatively charged and polar positively charged and polar
Certain enzymes catalyze the covalent linkage of an acetyl group to lysine amino acids as shown below. When a particular target protein is in the un-acetylated state, its interacting partner protein will not bind. However, once acetylated, the partner protein can bind to this target protein. Which of the following can you conclude? Select all that apply CH CO NH 3. NH Lysine acetylation reaction CH, CH, +HaN -C- CO- H. HIN-C- Co- H. UAcetylation changes the secondary structure of the target protein The partner protein has acidic residues in the interacting region Acetylation changes the tertiary structure of the target protein The partner protein has basic residues in the interacting region 8-1-8-8-8–8–d=
draw a “trans” and a “cis” peptide bond of alanine and threonine with the peptide bond lying in the plane of the paper. Draw a second view of each peptide bonds now looking down/along the peptide bond (i.e. one atom of the peptide bond will be in front and will obscure the second one behind it). Using a circular arrow, demonstrate how the torsion angle can be directly “read” from the picture. You can do this with an accuracy of ~10°. Provide an explanatory caption.

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Which of the following compounds is most similar to the transition state of peptide bond hydrolysis 7 A. R2 D. مدید ملی R2- HỎ .R1 B. ... E OH -RI