The amino acid sequence shown below is a short excerpt (residues 130-172) from the rod domain of ana-keratin-like protein. Predict the effect of each of the amino acid substitutions (stabilize, destabilize, no effect) andexplain your reasoning.130 - ATEFKTRFDDAALRANDIQL VIRSNEITADLIKDRLDQITTYY - 172a) Substitution of S in place of A at position 140.b) Substitution of V in place of I at position 147.

Following the rules of conservative amino acids, the amino acids that when replaced with a…

Answered: The amino acid sequence shown below is…

Organic And Biological Chemistry

7th Edition

ISBN:9781305081079

Author:STOKER, H. Stephen (howard Stephen)

Publisher:STOKER, H. Stephen (howard Stephen)

Chapter9: Proteins

Section: Chapter Questions

Problem 9.58EP

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Similar questions

Using both three- and one-letter codes for amino acids, write the structures of all possible peptides containing the following amino acids: (a) Val, Ser, Leu (b) Ser, Leu2, Pro
How many of the -amino acids shown in Table 26-1 contain aromatic rings? How many contain sulfur? How many contain alcohols? How many contain hydrocarbon side chains?
On complete hydrolysis, a polypeptide gives two alanine, one leucine, one methionine, one phenylalanine, and one valine residue. Partial hydrolysis gives the following fragments: Ala-Phe, Leu-Met, Val-Ala, Phe-Leu. It is known that the first amino acid in the sequence is valine and the last one is methionine. What is the complete sequence of amino acids?
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)
22-71 Which amino acid side chain is most frequently involved in denaturation by reduction?
A peptide has the sequence Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly The p?a values for the peptide’s side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side‑chain pKa glutamate 9.609.60 2.342.34 4.254.25 histidine 9.179.17 1.821.82 6.006.00 tryptophan 9.399.39 2.382.38 serine 9.159.15 2.212.21 glycine 9.609.60 2.342.34 leucine 9.609.60 2.362.36 arginine 9.049.04 2.172.17 12.4812.48 proline 10.9610.96 1.991.99 Calculate the net charge of the molecule at pH 11 and estimate the isoelectric point (pI)(pI) for this peptide.
Draw Tryptophan in a peptide bond. Explain all of the bonds using valence bond theory (VBT). Next, explain where VBT fails and how molecular orbital theory is a better description of key regions of this amino acid and the peptide bonds it forms with other residues
Determine the amino acid sequence of a polypeptide from the following data:Complete hydrolysis of the peptide yields Ala, Arg, Gly, 2 Lys, Met, Phe, Pro, 2 Ser, Tyr, and Val.Treatment with Edman’s reagent releases PTH-Val.Carboxypeptidase A releases Ala. Treatment with trypsin yields the following three peptides:1. Gly, Lys, Met, Tyr 2. Ala, Lys, Phe, Pro, Ser 3. Arg, Ser, Val
Using the information below, determine the amino acid sequence of the peptide, and explain how your structure is consistent with each piece of information. Complete hydrolysis by 6 M HCl at 110°C followed by amino acid analysis indicated the presence of Gly, Leu, Phe, and Tyr in a 2:1:1:1 molar ratio. Treatment of the peptide with1-fluoro-2,4-dinitrobenzene followed by complete hydrolysis and chromatography indicated the presence of the 2,4-dinitrophenyl derivative of tyrosine. No free tyrosine could be found. Complete digestion of he peptide with pepsin (which cleaves on the amino side of aromatic residues) followed by chromatography yielded a dipeptide containing Phe and Leu and a tripeptide containing Tyr and Gly in a 1:2 ratio.
Almost all proteins are composed from a set of about _____ amino acids.a. 4b. 10c. 20d. 50 ______ amino acids are considered essential.a. 5b. 10c. 15d. 20 An amino acid that has an indole group side chain.a. Trpb. Phec. Tyrd. ProWhich of the following is the simplest amino acid?a. Alab. Glyc. Vald. ProWhich of these will not give a blue solution with Ninhydrin testa. Prob. Phec. Alad. CysA neutral molecule with a positive and negative electrical charge.a. Isoelectric pointb. Zwitterionsc. Bufferd. Amphoteric3 amino acids joined together by two peptide bonds.a. Dipeptideb. Tripeptidec. Tetrapeptided. PolypeptideAn amino acid that can form disulfide bondsa. Cysteineb. Methioninec. Cystined. SerineWhich of the following is not a property of amino acidsa. Bufferb. Isoelectric pointc. Zwitterionsd. Insoluble in waterThe protein primary structure is held together bya. Hydrogen bondsb. Disulfide bondsc. Peptide bondsd. Protein bonds
The denaturing of proteins occurs when the stabilizing forces are altered. Below is the set of processes in which proteins are denatured. Classify the following processes according to the denaturing agent involved. Please help me understand the diff and correct any mistakes.
At very low pH, alanine is a diprotic acid that can be represented as H3N1-CH(CH3)-COOH. The pKa of the carboxyl group is 2.3, and the pKa of the UNH1 3 group is 9.7.(a) At pH 7, what fraction of the amino acid molecules dissolved in an aqueous solution will have the form H3N1-CH(CH3)-COO2?(b) What fraction of the molecules at this pH will havethe form H2N-CH(CH3)-COOH?

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