Hair is comprised largely of keratin, a fibrous protein consisting of two a-helices wrapped around eachother in a left-handed coiled-coil. The diagram below compares a partial alignment of the amino acidsequences of a form of human keratin and of ovine keratin. For each pair of dissimilar alignedamino acids, (i) indicate if a side chain is associated with a discrete charge by writing or (at pH 7)adjacent to the letter; and (ii) indicate whether each amino acid is polar (p) or apolar (a) in the caseof aligned, electrostatically-neutral, side chains. In the diagram, 219 and 158 designate se-quencepositions of the first aligned residue in each polypeptide strand.human II5 219ovine II7c 158FEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAEFEGYIETLRREAECVEADSGRLSSELNHVQEVLEGYKKKYEQEVALRATAE

Amino acids are biomolecules that have an amino group and a carboxyl group linked to the same carbon…

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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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The bacterially produced antibiotic gramicidin A forms channels in cell membranes that allow the free diff usion of Na+ and K+ ions, thereby killing the cell. This peptide consists of a sequence of Dand L-amino acids. The sequence of a segment of fi ve amino acids in gramicidin A is R-Gly-L-Ala-D-Leu-L-Ala-D-Val-R′. Complete the Fischer projection below by adding the correct group to each vertical bond.
Globular proteins are water-soluble, whereas fibrous proteins are insoluble in water. Indicate whether you expect the following amino acids to be on the surface of a globular protein or on the surface of a fibrous protein.(a) Ala (b) Glu(c) Leu (d) Phe(e) Ser (f) Val
Of the 20 protein-derived amino acids shown in Table 27.1, which contain Q.) no chiral center
The simplest form of the Ramachandran diagram is calculated by ignoring hydrogen bonding, interactions with water, and the hydrophobic effect. Why is this simple form of the diagram still an effective predictor of protein backbone conformation?
For the protein given in the attached picture: Write the name of these 5 amino acids corresponding to their abbreviation of 3 letters. Describe precisely how the functional groups in the amino acids are involved in bonding between two successive amino acids in the protein.
What would be the structural formula of the oligopeptide if the amino acids are arginine, glutamine, glycine, methionine and glutamic acid considering the first amino acid is the N-terminus
how does the protein environment surrounding an amino acid chain affect its chemical properties?Consider the carboxyl group on an asparate side chain in the following environments in a protein. Rank in order these environments from the highest to the lowest proportion of carboxyl groups in the -COO- form.that is in terms of pKas. 1. an aspartate side chain on the surface of protein with no other ionizable groups nearby. 2. an aspartate side chain buried in a hydrophobic pocket on the surface of a protein 3. an asparate chain in a hydrophobic pocket adjacent to a glutamte side chain 4. an asparate side chain in a hydrophobic porket adjacent to a lysine side chain.
Residues such as valine, leucine, isoleucine, methionine, andphenylalanine are often found in the interior of proteins,whereas arginine, lysine, aspartic acid, and glutamic acid areoften found on the surface of proteins. Suggest a reason forthis observation. Where would you expect to find glutamine,glycine, and alanine?
Sketch a titration curve for the following amino acids and indicate the pKa values for all titratable groups. Also indicate the pH at which this amino acid has no net charge. aspartic acid gly-val
Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU
A sample of the amino acid tyrosine is barely soluble in water. Would a polypeptide containing only Tyr residues, poly(Tyr), be more or less soluble, assuming the total number of Tyr groups remains constant?
Remembering that the amino acid side chains projecting from each polypeptide backbone in a β sheet point alternately above and below the plane of the sheet, consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg- Leu-Lys-Ile-Arg-Phe-Glu. Do you find anything remarkable about the arrangement of the amino acids in this sequence when incorporated into a β sheet? Can you make any predictions as to how the β sheet might be arranged in a protein?

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