6) Proline is not commonly found in the middle of a-helices because its ring structure prevents it fromadopting the proper value and because it disrupts the hydrogen-bonding pattern of the helix. Lookingat the structure of proline in the amino acid sequence below, suggest how this residue would disrupt thehydrogen-bondingpattern of an a-helix.'NHRNNH***R

A protein's function depends on its structure. There are four levels of protein structure: primary,…

Answered: 6) Proline is not commonly 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

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17. How would you computationally predict the thermodynamic stability of a long, extended RNA helix? Please explain in 1 sentence how structural "favorability" can be predicted
20. Nucleosides consist of a nitrogenous base bound by an N-glycosyl linkage to a phosphorylated pentose. true or false
1.Draw these phosphorylated structures as they would be connected in a polinucleotide (e.g.RNA) in the order A-B. / Show how they combine to form the polynuleotide (i.e. only the end product). Show at any one of these structures where the glycosidic bond occurs 2.Sanger sequencing revealed the sequence of an oligonucleotide to be: d-AGATGCCTGACT. Draw a diagram of the gel banding pattern post capillary electrophoresis i.e. where on the gel would the fragments feature
1 Draw the following polypeptide: Met- Tyr-Val-Ser-Asn 2A Draw the hydrolysis of a dipeptide consisting of phenylaline and glutamic acid. 2B What are the fuctional group present in the side chains of the amino acids.( phenylalanine and glutamic acid) 2C are the sidechains in part 2B hydrophobic or polar 2D where would you expect to find them ( surface or interior of a protein) ? why ?
(A) Give the polypeptide translation of the RNA sequence below. 5’-AUGGAAAUCAAAGUCAACCUUGAGUUUAGA-3’ (B) Write the chemical structure of the polypeptide sequence you determined in part (a) (C) Given the chemical structure of the polypeptide sequence you have written in part (b), answer True or False for each of the 5 statements below. (1) At least one of the amino acids in the sequence can undergo phosphorylation (2) The sequence looks like it could form a β turn (3) The sequence looks like it could form a β strand with one surface facing the interior of the protein and the other surface exposed to water (4) At least one of the amino acids in the polypeptide sequence can undergo oxidation to form a disulfide bridge to another polypeptide (5) The sequence looks like it could form an α helix that would be part of a coiled coil structure within a protein
I need help with drawing Hydrogen bonding between two tripeptide: Ser-Lys - Ser. In my class, we are required to give dash or wedge for the side chain R in the amino acid, and draw zig zag for the chain. In two separate drawings, can you draw one where it is the hydrogen bonding between the peptides backbone that connect the two tripeptides and the other is the hydrogen bonding between the side chains. Thanks
6 (a) A decapeptide has the following amino acid composition: Ala2 , Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides: Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly. Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine. From the experimental data, deduce the primary structure of the decapeptide. (b) Suggest a scheme you will follow to synthesize the dipeptide Ala-Gly
困 STRUCTURE AND NOMENCLATURE Name the fourth nucleotide from the 3' to 5' end. Use the How many terminal phosphate/s is/are present in the given structure? Give correct/appropriate punctuations, spacing and letter case based on the nomenclature. ONLY the NUMBER of the terminal phosphate/s. NH, O P-0 OP-O- OH 0=-0- NH: NH: NH; NH. 0=P-0- OH 0P-0- 0P-0- 0=P-0- OH 9:53 am P Type here to search 4) ENG 13/10/2021 近

Given the following diagram of how protein AWESOME1 binds to it's target DNA, describe the potential effects of each of the 5 mutations shown below. The wild-type sequence of a helix #1 is also shown in the blue box, and all the mutations are in helix #1 (see numbers for identifying particular residues). a helix #1 R(1)-V-I-L-Y-F-W-I-M-Y-F-S-H-Y-W-R(16) #1 Predict the consequence of the following mutations: 1) Arg(1) to Glu 2) Arg(1) to Ala 3) Phe(6) to lle 4) Trp(7) to Phe 5) Met(9) to Pro in
+H₂N-CH-COO™ T CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. O amino acid C amino acid D O amino acid E amino acid B +H₂N-CH-COO™ I CH₂ I CH₂ 1 O amino acid A C=0 B. If the pH decreases enough, this amino acid will become protonated and could contribute to the denaturation of the protein. +H₂N-CH-COO™ 1 CH₂ I OH C. +H₂N-CH-COO™ CH H₂C CH3 D.
1)If we were to begin with protein that is 145 residues long, How many (ATP/GTP) would have to be used? (ATP hydrolysis from 1 pyrophosphate= 2 ATP)' 2)What is the corresponding codon of an anticodon GUA (ignoring the wobble).
1. Consider the following α helix from myoglobin at pH 7. Gln-Gly-Ala-Met-Asn-Lys-Ala-Leu-Glu-His-Phe-Arg-Lys-Asp-Ile-Ala-Ala-Lys-Tyr(a) Label amino acids in the polypeptide above as follows: p for polar and uncharged, np for non polar, – for negatively charged, and + for positively charged.(b) How many complete turns are there in this helix?(b) Which side chains are likely to be on the side of the helix that faces the aqueous solvent? Why?(c) Which side chains are likely to face the interior of the protein? Why?

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