The bottom peptide segment is found in the secondary structure composed of anti-parallel - sheets. From the C-terminus of the peptide below, the sequence immediately after alternation contains the following amino acid residues (from N → C) A-F-R-M-Y-A. a) Although not listed here, what amino acids might be present at the section connecting the two anti-parallel (turn) strands? NH," HO Nterminus

The bottom peptide segment is found in the secondary structure composed of anti-parallel - sheets. From the C-terminus of the peptide below, the sequence immediately after alternation contains the following amino acid residues (from N → C) A-F-R-M-Y-A. a) Although not listed here, what amino acids might be present at the section connecting the two anti-parallel (turn) strands? NH," HO Nterminus

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

Give the sequence of the following tetrapeptide:
Identify the amino acids in the following peptides. Write it using the amino acid 3 letter abbreviation and the one letter code nomenclature. (Ex. Phe-Tyr-Trp FYW)
Draw three-dimensional representations of the following amino acids.(a) l-phenylalanine (b) l-histidine (c) d-serine (d) l-tryptophanDraw three-dimensional representations of the following amino acids.(a) l-phenylalanine (b) l-histidine (c) d-serine (d) l-tryptophan
Draw the structure of the tetrapeptide Asp-Arg-Val-Tyr. Please show the appropriate stereochemistry of the natural amino acids in the resulting peptide. Please draw all ionizable groups in their neutral form.
Anser the following questions for the peptides below
Part B Rank the following peptides from most to least hydrophobic. Rank the peptides from most to least hydrophobic. To rank items as equivalent, overlap them. • View Available Hint(s) Reset Help Asn-Arg-Ser-Arg-Asn Ser-Arg-Leu-Asn-Val Trp-Arg-Leu-Asn-Pro Trp-Leu-Arg-Pro-Leu Trp-Leu-Pro-Val-Leu Most hydrophobic Most hydrophilic
Inforior of 15.) The following sequence of amino acids occurs in a globular protein and forms an a-helix. Would you expect this section of the polypeptide to be located in the interior or exterior of the protein? Explain your answer. Leu-Ser-Phe-Ala-Ala-Ala-Met-Asn-Gly-Leu-Ala
Which of the following peptides have a net positive chargeat pH 7? (a) Gly-Ser-Lys, (b) Pro-Leu-Ile, (c) Phe-Tyr-Asp.
Imagine the main chain of a protein bends back on itself, so that two amino acid residues R₁ and R₂ come close to each other. Here's what R₁ loo -CH- CH₂ CH₂ CH₂ NH H₂N NH₂ Could R₁ form a salt bridge with R, at physiological pH, if R₂ were the right kind of residue? O yes O no If you said R₁ could form a salt bridge with R₂, what would R₂ have to be? 0 If there's only one possibility, write its 3-letter code. If there is more than one possibility, write the 3-letter code of any of them. X
Part B Consider the partial hydrolysis of the peptide Ala-Ser-Gly-Met-Thr-Val. Sort the smaller peptides according to whether they are are likely to form or if they will not form at all during this process. Drag each item to the appropriate bin. • View Available Hint(s) Reset Help Ala-Ser-Gly-Met-Thr Met-Thr-Val Ala-Ser-Gly-Met Ala-Met-Thr Gly-Met-Val Ser-Gly Gly-Met-Thr-Val Gly-Thr-Val Gly-Val Ser-Gly-Met-Thr-Val Likely to form Will not form
A peptide has the following amino acid composition: 2 Met, 2 Phe, 2 Glu, 1 Arg, 1 Lys, 1 Val, 1 Leu, 1 Gly, 1 Ser Reaction of the intact peptide with dansyl chloride followed by acid hydrolysis creates a derivative of Met. A specific cleavage of the intact peptide produces fragments with the following sequences: Fragment A: Glu-Gly-Lys-Phe Fragment B: Met-Ser-Leu-Arg Fragment C: Met-Val-Glu-Phe What information do this result give about the sequence of the peptide? Explain how you arrived on your answer. a) The sequence is: Met-Val-Glu-Phe-Glu-Gly-Lys-Phe-Met-Ser-Leu-Arg b) The sequence is: Met-Ser-Leu-Arg-Met-Val-Glu-Phe-Glu-Gly-Lys-Phe c) The sequence is: Met-Val-Glu-Phe-Met-Ser-Leu-Arg-Glu-Gly-Lys-Phe d) The sequence is: Met-Ser-Leu-Arg-Glu-Gly-Lys-Phe-Met Val-Glu-Phe
His-Met-Asp-Tyr-Phe-Ser within this peptide, which amino acid residue is the most hydrophobic and why?