Which of the following statements about alpha-helix and beta-sheet structure are true? More than one answer is correct. -they are aspects of protein secondary structure. -they are maintained by hydrogen-bonding interactions within the polypeptide backbone. -most proteins fall into one of two categories: those composed entirely of alpha-helix, and those composed entirely of beta-sheet. -in both alpha-helix and beta-sheet, each amino acid (at position n) interacts with another amino acid at position n+4. -alpha-helix contains only hydrophobic amino acids, while beta-sheet contains only hydrophilic amino acids

Which of the following statements about alpha-helix and beta-sheet structure are true? More than one answer is correct. -they are aspects of protein secondary structure. -they are maintained by hydrogen-bonding interactions within the polypeptide backbone. -most proteins fall into one of two categories: those composed entirely of alpha-helix, and those composed entirely of beta-sheet. -in both alpha-helix and beta-sheet, each amino acid (at position n) interacts with another amino acid at position n+4. -alpha-helix contains only hydrophobic amino acids, while beta-sheet contains only hydrophilic amino acids

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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Which of the following statements are true? The local folding of the polypeptide in some regions gives rise to the secondary structure of the protein. The most common secondary structures are the α-helix and β-pleated sheet structures. Certain amino acids have a propensity to form an α-helix, while others have a propensity to form a β-pleated sheet. Select the correct answer below: 1 and 2 1 and 3 2 and 3 all of the above
Which of the following is primarily responsible for stabilizing the a-helix, a type of 1. secondary structure formed by a single nolvpeptide chain? hydrophobic interactions hydrogen bonds of backbone ionic interactions disulfide bridges hydrogen bonds involving the R-side chains a) b) atoms d) The atoms that make up the peptide bond that links amino acids together in a protein are in the same plane (coplanar). In the a-helix, how are these peptide bond planes arranged? 2. a) perpendicular to the a-helix approximately parallel to a-helix axis b) both parallel and perpendicular to the a-helix randomly oriented with respect to the axis of the a-helix peptide bond planes don't exist in the a-helix
A mutation leads to a change in amino acid from valine, an amino acid with a nonpolar side chain, to aspartic acid, an amino acid with a polar, negatively-charged side chain. Do you think that the following levels of protein structure change? If so, how and why? If not, why not? Please frame your answer in terms of chemical bonds and interactions. (primary structure, secondary structure, tertiary structure, quartenary structure)
Oftentimes, the major challenge in the determination of protein structure via X-ray crystallography is the production of good crystals. One common approach is to crystallize fragments of the whole protein instead of crystallizing the whole protein. If you were to cleave a protein into fragments that will still retain the folding of that fragment in the whole protein, where is the best location to perform the cleavage? O At the ends of each alpha helix. O At the ends of a protein motif. O At the points connecting protein domains. O At the ends of beta strands.
Protein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct? 1) the folding pattern of a protein is ultimately determined by its amino acid sequence. 2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface. 3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains. 4) the overall folding pattern/shape of a protein molecule is termed its primary structure. 5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence. More than one answer might be right
Proteins are found to have two different types of secondary structures viz. a-helix and B-pleated sheet structures. a-helix structure of a protein is stabilised by: (i) Hydrogen bonds (ii) van der Waals forces (iii) Peptide bonds (iv) Dipole-dipole interactions
You have a section of a protein that has the following amino acid sequence: GPMG What is full name of the N-terminal amino acid residue? Just type the name (one word). What is the full name of the amino acid residue immediately N-terminal to the most C- terminal amino acid residue? Just type the name (one word). What secondary structure is this most likely to form, according to the Chapter 4 reading? (One word answer.)
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
β-pleated sheets and α-helices arise more from interactions in the peptide backbone than from the “R” groups of the individual monomers; they are examples of the (????) structure of a protein. Primary Tertiary Secondary Quaternary (????) are comprised of a nitrogenous base, a pentose sugar, and a phosphate group. Monosaccharides Amino acids Proteins Nucleotides (????) is the RNA transcript of the DNA sequence that determines the primary structure of a protein. mRNA lncRNA tRNA rRNA If a substance such as a lipid isn’t soluble in water it might be described as (????) Hydrophilic Hydrophobic
There are different types of helical structures that can be found in proteins (i.e., not only helices). What is common among different types of helices is that the he structure is maintained by intrachain hydrogen bonding between two polypeptide backbone atoms. Oftentimes, at least two intrachain hydrogen bonds need to be formed in order for a helix to start gaining stability. This can be observed from circular dichroism, technique that detects helicity in proteins. Circular dichroism starts detecting helicity in a helical chain only when there are at least two intrachain hydrogen bond formed. If a helical structure is too short such that it only has one intrachain hydrogen bond, the helix is too unstable for the helicity to be accurately detected th circular dichroism. Four different types of helical structures were studied using circular dichroism and the minimum number of residues needed for helicity to become detectable wa determined as summarized in the table below. Minimum number…
Which of the following best describes how the secondary structure of a protein is formed? A B с D O=U a-helix H O=C N-H R-C-H C=0 H-N H-C-R O=C N-H R-C-H C=O H-N O-C N-H R-C-H C=O H-N N-H 0= H-C-R H-N C=O R-C-4 N-H O=C H-C-R 4-1 Ç=O R-C-H N-H 0=C H-C-R (=O R-C-H B-pleated sheet ionic bonds between the R groups of the polypeptide amino acids -Uh hydrogen bonds between the carboxyl and amino groups of non-adjacent amino acids covalent bonds between the carboxyl and amino groups of adjacent amino acids hydrogen bonds between the R groups of the polypeptide amino acids
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