нн.N-C-CНН.N-C-CClassify the following amino acid2.ноннонсн.ÇH2CH,ÇH2CH.structureонBased on Chirality• Based on Configuration• Based on R-group (side chain)NHннC-NBased on Acidic – Basic3.H,NноНсн,сн,property• Based on PolarityBased on EssentialityIdentify the name of the amino acidCHв ОCH34.НО1.НаСОНNH2NH25. • Give the name of each amino acidClassify the peptideDipeptide, Tripeptide, Polypeptide or ProteinGive the name of the peptide• Using amino acid name, 3 letter and 1 letter abbreviationОнCH, CнCHCH-он н нH CH2НCH3H CH2H,N-CC-N-CC-N-C-C-N-C-COOНН

“Since you have asked multiple question, we will solve the first question for you. If you want any…

Answered: н н. N-C-C Н Н. N-C-C Classify the…

World of Chemistry, 3rd edition

3rd Edition

ISBN:9781133109655

Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCoste

Chapter21: Biochemistry

Section21.1: Introduction To Proteins

Problem 3RQ

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Similar questions

A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)
What special role does the amino acid cysteine have in the peptides vasopressin and oxytocin?
Describe in words the hydrogen bonding that occurs in a protein having an -helix secondary structure. A top view of an -helix, looking down the long axis, shows how the side chains green point away from the axis.
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. I.e Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though…
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. Why n→π* interactions contribute more to the overall stabilization of the protein than Sulfur-arene interactions, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Anion-π interactions, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Chalcogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than X-H-π interactions, even…
As we’ve discussed, a peptide bond is made when amino group of one amino acid combines with the carboxylic acid group of another amino acid (releasing a water molecule in the process). The C-N bond formed in this process is called a peptide bond. Peptide bonds have a few properties that might be unexpected. b) Another observation is that although the N-H of the peptide bond is able to serve as a H-bond donor the N atom of the peptide bond does not serve as an effective H-bond acceptor. Provide an explanation for this observation, using Lewis structures, VSEPR theory and/or valence bond theory as appropriate.c) It is also fairly accepted that while proteins undergo dynamic motions and conformational changes, and while R groups can freely rotate about Cα, it is generally not possible to freely rotate around a peptide bond. Please explain this observation, using a picture showing relevant orbitals on relevant atoms (your answer for part (a) might provide a useful basis for your reasoning…
Draw a sawhorse projection for 3-aminobutan-2-ol representing where the two CH3-groups are syn-periplanar to each other.
Lysine and tryptophan are two amino acids that contain an additional N atom in the R group bonded to the α carbon. While lysine is classified as a basic amino acid because it contains an additional basic N atom, tryptophan is classified as a neutral amino acid. Explain why this difference in classification occurs.

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