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.

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.

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 24QP: a. Can a mutation change a proteins tertiary structure without changing its primary structure? b....

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You are working in a bioengineering lab, and you are asked to create a peptide with a helix with length of 3 nm, a beta strand with length of 35 Å, and a linker containing 25 amino acid residues. a. How many amino acid residues are in this peptide? b. What is the mass of the peptide? 2. Why is quinary structure necessary for a full understanding of how drugs work in cells?
Which is a difference between an alpha-helix and a beta-pleated sheet? Select one: a. An alpha-helix contains mainly amino acids with polar R-groups while a beta- pleated sheet contains mainly amino acids with non-polar R-groups. b. An alpha-helix contains disulfide bonds while a beta-pleated sheet contains ionic bonds. c. An alpha-helix has non-covalent bonds between amino acids near each other in the sequence while a beta-pleated sheet has non-covalent bonds between amino acids far apart in the sequence. d. An alpha-helix has a spiral shape while a beta-pleated sheet has a compact zig-zag shape.
Describe why G-C bonding is stronger than A-T. Why is it important?
Valine is an amino acid with a nonpolar side chain and serine is one with a polar side chain. Draw the two amino acids.(a) Why is the side chain for valine nonpolar, whereas the side chain for serineis polar?(b) Which amino acid has a hydrophilic side chain and which has a hydrophobic sidechain?
Use a rough diagram to compare the structures of a proteina-helix and an antiparallel b-sheet. For simplicity, showonly the backbone atoms of the protein.
Draw the resonance structure of a tripeptide peptide backbone, indicating the N- and C-terminaland give e
How do you answer this question: Describe the 'peptide backbone' of a polypeptide. How are the 'R' groups oriented along the peptide backbone of a polypeptide?
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. Where would you expect valine, leucine, and isoleucine to be located in a polypeptide? (Inside or outside)? Explain your answer using the properties of the amino acids listed. B.How would your answer change, if the amino acids were Lysine and Histidine?
a) Draw a non-covalent interaction between a water molecule and the charge on a phosphorylated serine residue(not including backbone atoms). What type of interactuon is this, how strong is it, and what holds the interaction together? b)Draw a non-covalent interaction between an alanine residue and a valine residue(not including backbone atoms). What type of interaction is this, how strong is it, and what holds the interaction together?
A peptide has the sequence (a) What is the net charge of the molecule at pH 3, 8, and 11? (Use pKa values for side chains and terminal amino and carboxyl groups )(b) Estimate the pI for this peptide.
1. (a) Draw a circle around one amino acid in the structure. (b) Draw a box around one amino acid side chain. (c) Indicate whether the side chain you chose is hydrophobic or hydrophilic. (d) Draw an arrow pointing to a peptide bond 2. If the peptide segment shown above was part of a beta sheet, which of its functional groups would be involved in forming and stabilizing the beta sheet? 3. Which amino acid (also called amino acid residue)would be more likely to occur on the surface of a protein: an aspartate residue or a methionine residue? Explain your choice.