An a helix would be destabilized MOST by○ a glycine residue adopting alpha-helical backbone dihedral angles○ interactions between neighboring Asp and Arg residues○ interactions between two adjacent hydrophobic Val residuesO the presence of an Arg residue near the carboxyl terminus of the a helixO the presence of two Lys residues near the amino terminus of the a helix

The stability of an alpha-helix is influenced by various factors including the propensity of amino…

Answered: An a helix would be destabilized MOST…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 19QP: Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the...

See similar textbooks

Similar questions

Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.
The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are: a. always side by side. b. generally near each other in sequence. c. invariably restricted to about 7 of the 20 standard amino acids. d. often on different polypeptide strands. e. usually near the polypeptide chain's amino terminus or carboxyl terminus.
In the alpha-helices, which of the following statement is NOT true? a. Backbone carbonyl oxygen of residue (i) hydrogen bonds to backbone NH of the fourth residue of chain of residue (i + 4). b. Side chains project out from an α-helix. c. Hydrogen bonds are almost straight and parallel to the helix axis. d. Helix has a macrodipole. e. The rise or advance per amino acid residue is 0.54 nm.
An a-Helix (or helices) is often found at anion binding sites of different proteins. Explain this observation using a schematic drawing of a-helix. Clearly indicate the direction of the dipole and the N-terminus of the helix. Show the structure of the functional group of the glutamic acid side chain in its (general) base form.
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.
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?
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?
Draw the structure of the dipeptide Thr-Cys at pH7. Clearly indicate the following: the amino terminus (N) the carboxyl terminus (C) a peptide bond an α-carbon atom
What following statement is TRUE concerning motifs and domains? a) Both motifs and domains are independently stable. b) Domains undergo dynamic individual changes that affect the entire protein c) B-a-ß loops, B barrels, and helix-turn-helix structure are types of domains d) Motifs and domains are part of secondary structural elements e) Ab initio computations predict motif folds accurately a majority of the time My guess is B.
How can you describe the hydrogen bonding pattern of alpha helices? a. NH of residue n with CO of residue n+3 b. CO of residue n with NH of residue n+3 c. NH of residue n with CO of residue n+4 d. CO of residue n with NH of residue n+4
In the image attached, there are 4 nitrogenous bases plus ribose used to generate strands of DNA. They are oriented with hydrogen bonding regions aligned. Diagram the enol form of cytosine following a tautomeric shift. Include in the diagram how this change shifts hydrogen bonding characteristics and a new binding partner for this nucleotide.
The tertiary structure of a protein is maintained by interactions between the side chains of amino acid residues one such interaction is between cysteine residues, sketch a covalent bond link that can form between side chains of two cysteine residues. Only relevant atoms that can form the link need to be shown

SEE MORE QUESTIONS

Recommended textbooks for you

Human Heredity: Principles and Issues (MindTap Co…

Biology

ISBN:

9781305251052

Author:

Michael Cummings

Publisher:

Cengage Learning