Select the true statements about protein secondary structure.In an a-helix, the side chains are located on the outside of the helix.The secondary level of protein structure refers to the spatial arrangements of short segments of the protein.In a B-pleated sheet, the side chains are located between adjacent segments.Peptide bonds stabilize secondary structure.The x-helix is held together by hydrogen bonds between the amide N-H and C=O groups.Incorrect

The polypeptide chain undergoes folding in order to acquire a three dimensional conformation that is…

Select the true statements about protein secondary structure. In an a-helix, the side chains are located on the outside of the helix. The secondary level of protein structure refers to the spatial arrangements of short segments of the protein. In a ß-pleated sheet, the side chains are located between adjacent segments. Peptide bonds stabilize secondary structure. The a-helix is held together by hydrogen bonds between the amide N-H and C=O groups.

Select the true statements about protein secondary structure. In an a-helix, the side chains are located on the outside of the helix. The secondary level of protein structure refers to the spatial arrangements of short segments of the protein. In a ß-pleated sheet, the side chains are located between adjacent segments. Peptide bonds stabilize secondary structure. The a-helix is held together by hydrogen bonds between the amide N-H and C=O groups.

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 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
It is often the case that a helices are positioned in a protein such that one side faces the interior of the protein and the other, the surface of the protein. These are said to be amphiphilic helices because they face different environments. Using a helical wheel projection (shown below), which of the peptide(s) below might form an amphiphilic helix? 8 15 1 12 4 11 16 18 9 7 14 13 10 17 O SLIKSVIEMVDEWFRTFL O FLIRVLRKVFRVLTRILS O RLFRSRVLKIAVIRFLLI
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
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…
The different types of interactions that stabilize the protein tertiary structure are illustrated in the diagram below. Which type of interaction moves some part of the polypeptide chain toward the inside of the folded protein? OH Hydrophilic OH CH₂ interaction with water Hydrogen bond -NH₂3-0- C Salt bridge -CH₂-OH C=0 H-N H 0-CH,- I H Hydrogen bond Salt bridge O Disulfide bond 222 -SIS Hydrophobic interaction 200 O Hydrogen bond O Hydrophilic interaction Disulfide bonds B-Pleated sheet O Hydrophobic interaction CH₂ CH₂ a Helix CH3 CH3 Hydrogen bonds
Match the protein structure terms on the left with the descriptions on the right. v (Choose ) commonly observed combinations of secondary structural elements tertiary structure Long segments of secondary structure. supersecondary structure basic component of quaternary structure Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the peptide Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the side chain compact structural or functional regions within a given polypeptide functional structures formed by non-covalent interactions between multiple polypeptides. domain (Choosel subunit quaternary structure (Choose)
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
A helical wheel is a two-dimensional representation of a helix, a view along its central axis. Label the blanks on the helical wheel diagram to show 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- 1 Answer Bank H L D K R F T K S T
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. More than one answer is correct I am confused
Which statement best describes the protein structure shown below? This is an alpha helix. This is a tertiary structure that consists almost entirely of beta strands. This is a tertiary structure consisting of a roughly equal mixture of alpha helices and beta sheets. This is a beta sheet. This is a tertiary structure that consists almost entirely of alpha helices.
The primary structure of a protein is shown below. Please answer the following questions. Leu-Arg-Ser-lle-Glu-Thr-Val-Val-Asn-Gln-Val-lle-Ser- Tyr a. Where is this section of the polypeptide most likely located [ Select ] completely embedded inside the protein partially exposed to the aqueous environment b. Is the above more likely an alpha helix or a beta-pleated sh completely exposed to the aqueous environment c. Which two amino acid residues are least likely to be in an alpha helix, but most likely to be a part of a beta turn? (Please select the amino acids in alphabetical order). [ Select ] [ Select ]
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