Which of the following is incorrect about the beta-sheet? a. The strands in anti-parallel beta-sheets are usually connected with turns b. Side chains are alternated above and below the sheet C. Parallel beta-sheets are less stable than the anti-parallel ones Od. It is stabilized by hydrophobic interactions between the side chains of nonpolar residues

Which of the following is incorrect about the beta-sheet? a. The strands in anti-parallel beta-sheets are usually connected with turns b. Side chains are alternated above and below the sheet C. Parallel beta-sheets are less stable than the anti-parallel ones Od. It is stabilized by hydrophobic interactions between the side chains of nonpolar residues

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

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The β-Sheet is formed mainly by a. hydrophobic interaction b. hydrogen bonding between the peptide bond and water c. hydrogen bonding between two strands d. hydrogen bonding of the side chains e. disulfide bonding
Which of the following is FALSE? Select one: a. The hydrogen bonding in a beta-sheet is between strands rather than within strands. b. The two main types of secondary structure are the alpha-helix and beta-sheet structures c. The hydrogen bonding in a beta-sheet is within strands rather than between strands. d. Alpha-helix is maintained by hydrogen bonds.
Which of the following is NOT an example of protein secondary structure? a. alpha-helix b. beta sheets c. beta turn d. coiled coil e. loops
Which of the following best describes how the large and branched side chains are organized within a beta-sheet? a. They are kept near each other. b. They are kept far apart from each other. c. They alternate every other residue. d. They organize parallel to each other in consecutive polypeptide chains.
What is the primary driver of protein folding on a macro level? a. Hydrogen bonding b. Van der Waals forces c. Covalent bonding d. Entropic force
Proteins denature at low pH. What characteristic of acidic environments interferes with protein folding? A. The lack of protons in the solution breaks covalent bonds in the protein. B. The excess protons in the solution break covalent bonds in the protein. C. The lack of protons in the solution breaks hydrogen bonds in the protein. D. The excess protons in the solution break hydrogen bonds in the protein.
Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
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.
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.
Which of the following statement about proteins is correct a. alpha helix and Beta pleated sheets are considered quaternary structures b. a single polypeptide only has primary sytructure, secondary, tertiary, and quaternary structures require more than one polypeptide c. there are 30 essential amino acids that are the monomer building blocks of proteins d. polypeptides have a distinct polarity (directionality) with one end refered to as the free amino end, and the other called the free carboxyl end
Which of the following statements are correct about the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic interactions
The amino sequence of a protein is: alanine, leucine, valine, threonine. This information reveals the protein’s _______ structure. The “C” terminus or side of this protein is ______. Select one: a. primary, alanine b. secondary, alanine c. secondary, leucine d. secondary, threonine e. primary, threonine