Which of the following is true about formation of the secondary structure features, a-helices or a B- sheets? O Their formations are enthalpically favored because they are largely stabilized by H-bonding Their formation is entropically unfavored because their formation restricts the rotational and translational motion of the constituent amino acids O Their formation is entropically favored because of the hydrophobic effect

Which of the following is true about formation of the secondary structure features, a-helices or a B- sheets? O Their formations are enthalpically favored because they are largely stabilized by H-bonding Their formation is entropically unfavored because their formation restricts the rotational and translational motion of the constituent amino acids O Their formation is entropically favored because of the hydrophobic effect

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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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.
Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
Which of the following statement is not true? In a secondary structure the consecutive residues have phi and psi values that are quite different. The Ramachandran diagram defines the restrictions of polypeptide backbone conformation. Two α helices with hydrophobic side chains repeated in a regular pattern can form dimeric structures in water. Greek key motifs occur frequently in antiparallel β structures. Both α helices and β sheets can be amphipathic.
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.
Proline is known as a beta sheet and alpha helix "breaker ," therefore proline is rarely found in beta sheets or alpha helices. why do you think this is? In your explanation, you should describe the specific molecular interactions necessary for the formation of alpha-helices and beta-sheets. Please be as specific as possible.
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
Show below is a polypeptide comprised of 3 α-helices and 5 β-sheets joined by randomcoil. Characterizetheforces that stabilize the tertiarystructure and draw the interacting side chains ofd) Cys Cys
Which of the following statements are correct about the molten globular state of protein folding (select all that appy)? A. May be short-lived or long-lived intermediate in protein folding B. Contains substantial levels of secondary structure C. Has loose packing of hydrophobic core D. Larger radius of gyration than dentaured state E. Is a more compact state than the native confomation
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
In the peptide Ala – Gly – Val – Phe – Tyr, a carboxylate (-COO-) group would bound in which amino acid? A) Gly b) Ala c) Phe d) Tyr Which amino acid forms disulfide bonds? A) Met b) Cys c) Arg d) Pro The sequence Gly-Pro-Pro is often found in collagen. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure
it is widely accepted that proteins can organize themselves according to a range of stable structural motifs. How is this knowledge exploited in the organization of the protein data blank?
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?