An π helix can be described as a 4.4, helix. Explain16what this designation means. Given the pitch of thehelix is 5.2 angstroms, how long in(nm) is the pi helixthat has six residues.

●A π helix is a type of secondary structure found in proteins.The amino acids in a standard π-helix…

Answered: An π helix can be described as a 4.4…

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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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?
Helices can be described by the notation nm,where n is the number of residues per helical turn and m is the number of atoms, including H, in the ring that is closed by the hydrogen bond. Would a 310 helix be more or less steep than an α helix? why?
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.
Polyglycine, a simple polypeptide, can form a helix with φ = -80°, ψ = +150°. From the Ramachandran plot (as shown), describe this helix with respect to handedness.
The pi-helix is a rare secondary structural element in proteins that resembles an alpha helix but has slightly different properties. Notably, hydrogen bonds within a pi-helix display a repeating pattern in which the backbone C=O of residue i hydrogen bonds to the backbone HN of residue i+5. Based on this information, which of the following are true? Select all that apply. O The hydrogen bonding distance between C=O and NH groups remains unchanged between pi-helices and alpha-helices The torsion angles of amino acids found in pi-helices are the same as those found in alpha-helices Pi-helices have a smaller rise per residue compared to alpha- helices Pi-helices have fewer residues per turn compared to alpha-helices Pi-helices have more residues per tůrn compared to alpha-helices Pi-helices are left handed
What is the length (in nm) of an alpha-helix containing 15 amino acid residues?
Define alpha (a) helix
Part B Assume a protein is composed of 120 amino acid residues and that each amino acid can have three possible orientations. How many total possible orientations are there for the protein? Express the number of possible orientations to three significant figures. —| ΑΣΦ 1.797 • 1057 Each possible orientation of an amino acid is due to rotation about a bond. Since there are two terminal amino acids, there will be one fewer peptide bond compared to the number of amino acids. No credit lost. Try again. Submit ? Previous Answers Request Answer orientations
Alpha-helices have 3.6 amino acid residues per turn, ie a helix 36 amino acids long would form 10 turns, and The axial distance between adjacent residues is 3.5 Angstroms. Beta-helices have two residues per repeat unit which gives the beta-strand a 7 Angstrom pitch. This compares with the alpha-helix where the axial distance between adjacent residues is only 1.5 Angstroms. Then how many residues in an alpha-helix conformation would it take to traverse the same distance as 10 residues in beta-strand conformation?
(a) NMR measurements have shown that poly- L -lysine is a random coil at pH 7 but becomes a helix as the pH is raised above 10. Account for this pHdependent conformational transition. (b) Predict the pH dependence of the helix–coil transition of poly- L - glutamate
TERTIARY STRUCTURE (A) (B) (C) Fg Eet Galand Sen 20e Figure 6. Examples of the arrangement of a-helices and B-sheets in folded protein domains. Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission of Garland Science/ Taylor & Francis LLC. Figure 6 shows three examples of how secondary structure elements can be arranged in relation to one another in the functional, folded form of a complete protein or one compact portion of a protein. The overall three-dimensional shape (or conformation) of a protein is its tertiary structure. • What do you think holds together the various secondary structural elements in a particular three-dimensional pattern? (Hint: Look back at Figure 5 - what is sticking out from the sides of the a-helices and B-strands?)
Using a copy of a helical wheel (attached to the end) plot the amino acids of the helix on the helical wheel. Is there any evidence of the helix as a whole being amphipathic or having a “sidedness"? Explain yes or no. Are the amino acid side chains in close proximity of one another or staggered to minimize steric hinderance between side chains? Explain the pattern you observe.

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An π helix can be described as a 4.4 helix. Explain 16 what this designation means. Given the pitch of the helix is 5.2 angstroms, how long in(nm) is the pi helix that has six residues.