I would appreciate help The carbon-nitrogen peptide bond is rigid, but rotation can180take place about the N-Cq and the Ca-C bonds in a protein(Ca is the a carbon atom). These bond angles define the120conformation of the peptide chain.60Consider the Ramachandran plot to answer both questions.Which observation most likely describes part of an-60observed a helix?-120O p = -59°; y = +150°; many Ser residues$ = +60°; y = +40°; many Gly residues-180-180180p = -57°; y = -47°; many Pro residues$ (degrees)p = -60°; y = -47°; many Ala residuesO p = -140°; y = +130°; many Val residuesO O$ (degrees) Which observations would not likely occur in a ß sheet?$ = +60°; y = +60°; many Gly residues0 = -139°; yy = +135°; many Val residuesp = -51°; y = +153°; many Gly and Pro residues$ = -57°; y = -49°; many Ala residuesp = -120°; w = +120°; many Tyr residues

The proteins are polypeptide chains of amino acids. These amino acids are packed into protein…

Answered: Consider the Ramachandran plot to…

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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An unspecified protein contains a 15-residue long α-helix with the following sequence: WEANIKQRLSTMGEYKQCHANG a. How many full turns are there in this α-helix? b. What is the length of the helix (in Angstroms) in the direction of the helix axis? c. How many hydrogen bonding interactions would be there in this α-helix? d. If it was a 310 helix instead with a helical pitch of 6 Å, is it long enough to span the 30 Å bilayer? Calculate and explain.
The structure of an alpha helix orients the oxygens of the carbonyl group of the peptide bond towards the C-terminal end of the helix while the hydrogens of the NH groups orient toward the N-terminal end, thus imparting a dipole along the length of the helix. As a result, which kinds of amino acids would favor the C-terminal end, and which would favor the N-terminal end? negatively charged, positively charged positively charged, negatively charged negatively charged, hydrophobic positively charged, hydrophobic hydrophobic, negatively charged hydrophobic, positively charged
Consider the following peptide to answer the questions below: A M A K K E S H I F T A I D E What is the total charge of this peptide at pH = 5? What is the N terminal amino acid (full name)? C terminal amino acid? How many fragments would result if this peptide underwent proteolytic cleavage with V-8 protease and what are these fragments (list them)? Would this peptide be a candidate to form an alpha helix? Why or why not
The unfolding of the α helix of a polypeptide to a randomly coiled conformation is accompanied by a large decrease in a property called specific rotation, a measure of a solution’s capacity to rotate circularly polarized light. Polyglutamate, a polypeptide made up of only L-Gluresidues, has the α-helix conformation at pH 3. When the pH is raised to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (L-Lys residues) is an α helix at pH 10, but when the pH is lowered to 7 the specific rotation also decreases, as shown by the following graph. What is the explanation for the effect of the pH changes on the conformations of poly(Glu) and poly(Lys)? Why does the transition occur over such a narrow range of pH?
A helical wheel is a two-dimensional representation of a helix, a view along its central axis Use the helical wheel diagram shown here to determine the distribution of amino acid residues in a helical segment with the sequence –Val–Asp–Arg–Val–Phe–Ser–Asn–Val–Cys–Thr–His–Leu–Lys–Thr–Leu–Gln–Asp–Lys–What can you say about the surface properties of this helix? How would you expect the helix to be oriented in the tertiary structure of an integral membrane protein?
Which of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (B) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (E) They require a high content of proline and glycine
A short peptide of about 15 amino acids contains 3 Leu, 6 Val, and 3 Thr. What secondary structure is it most likely to adopt? Please answer with detailed reasonings. a. beta-sheet b. random unstructured coil c. hairpin turn (reverse turn) d. helix.
Given that an α helix has 3.6 residues per turn and the rise along the α helix axis is 5.4 Å, approximately how many amino acids would you find in a single contiguous α helix that is 210 Å long?
What is the primary reason the a-helix conformation in polypeptides such a stable form? A. The a-helix structure is stabilized by hydrophobic interactions. B. The a-helix structure is stabilized by intra-helical hydrogen bonds. C. The a-helix structure is stabilized by disulfide bonds. D. The a-helix structure is stabilized by proline residues.
Which of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (8) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (€) They require a high content of proline and glycine
Regarding the last answer choice, how come both alpha helices and beta sheets aren't denatured when the heat breaks peptide bonds? If heat were to break peptide bonds, wouldn't that affect the primary structure which inevitably affects the more complicated structures?
the amino acid histidine has three ionizable groups with pKa values of 1.8, 6.0, and 9.2. In a solution at PH 5.4 what percentage of the histidine side chains will carry a postive charge?

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