Which of the following is true about a peptide bond:Electron delocalization occurs between the a-amino group of one residue and the a-carbon ofthe subsequent residueThe peptide bond is freely rotatable along its bond axisThe peptide bond contains 5 co-planar atomsDehydration to link two residues occurs due to thermodynamic coupling to high-energyphosphate hydrolysisNone of the answers are correct

A peptide bond is formed between the α-nitrogen atom of one amino acid and the carbonyl carbon of…

Answered: Which of the following is true about a…

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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Similar questions

Answer the following questions based on the structure of the following peptide and the information in the attached table of enzyme activities. M-F-V-W-E-Q-A-P-S-P-L The charge of this peptide at pH 7 would be
Which of the following is not true about a-amino acids? have at least 2 pka values O negatively charged at pH = 1.0 most contain one chiral center can act as buffers
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 way is more common practice to characterize the strength of a binding reaction between a protein and its ligand? Group of answer choices By its binding free energy, delta G By its equilibrium association constant K(A) By its equilibrium dissociation constant K(D) By the rate at which the biding reaction proceeds
Which of the following amino acids would be MOST likely used as a nucleophile in a reaction mechanism? Ala Trp O Cys Ile QUESTION 37 Investigating how protein subunits come together studies: quaternary structure tertiary structure super- secondary structure primary structure QUESTION 38 Mey coy Click Save and Submit to save and submit. Click Save All Answers to saue all 4nswers
Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn Erase
Create an oligopeptide via dehydration synthesis using the following amino acids trp and gly
Glutamate ,tryptophan,leucines,tyrosine, phenylalanine Which of the following amino acid is the most soluble in water at pH7 & why?
Sketch the following two tripeptide chains: Asp-Gly-Ser and Ile-Asn-Met at physiological pH . Please provide only typed answer solution no handwritten solution needed allowed
Which of the following amino acids has a net negative charge at physiologic pH (~7.4)? Lysine Asparagine O Histidine O Glutamic acid
In terms of structure and function of a protein why is the lactase enzyme have a optimal pH of seven
Which of the following amino acids have R groups that have hydrogen- bonding potential? Ala, Gly, Ser, Phe, Glu, Tyr, Ile, and Thr

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