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...

See similar textbooks

Related questions

Q: Describe the general structure of a type 2 alpha helix protein. Explain how type 2 alpha helix…

A: The - (alpha) helix and the - (beta) sheet are the two most prevalent secondary structures…

Q: On which of the following amino acids is an N-linked glycan added to? A.Asparatic acids…

A: Basic amino groups (-NH2) and carboxyl groups (-COOH) are found in amino acids. Proteins have amino…

Q: a) Draw a non-covalent interaction between a water molecule and the charge on a phosphorylated…

A: Unlike covalent interactions where there is sharing of electrons between two atoms, in non-covalent…

Q: latch the following examples with the levels of protein structures. 4 1 2 3 > > The overall fold of…

A: All the structures given below show different levels of protein structure such as primary,…

Q: I'm working on the thermodynamics of protein binding but I want to understand more on the enthalpic…

A: Introduction Protein folding and protein-ligand interaction are basically thermodynamically driven…

Q: Two proteins are discovered, and both are shown to have a potential in treating fatty liver…

A: There are few points fatty liver syndrome . These are as follows : We know that fatty liver…

Q: Which of these peptides is the most hydrophobic? A. KFYV B. ERSC C. PIMF

A: Proteins are modified polypeptide chains. These chains are made up of 10 or more amino acids linked…

Q: Consider the following protein sequence as an α helix:…

A: The sequence and identity of amino acids of a polypeptide chain make its primary structure.

Concept explainers

Proteins

We generally tend to think of proteins only from a dietary lens, as a component of what we eat. However, they are among the most important and abundant organic macromolecules in the human body, with diverse structures and functions. Every cell contains thousands and thousands of proteins, each with specific functions. Some help in the formation of cellular membrane or walls, some help the cell to move, others act as messages or signals and flow seamlessly from one cell to another, carrying information.

Protein Expression

The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry, and protein research laboratories.

Question

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

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

This is a popular solution!

SEE SOLUTION Check out a sample Q&A here

Step 1

VIEW

Step 2

VIEW

Trending now

This is a popular solution!

Step by step

Solved in 2 steps

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.

Similar questions

Which of the following is incorrect about the beta sheet? Parallel beta sheets are less stable than the anti-parallel ones O b. It is stabilized by hydrophobic interactions between the side chains O c. The strands in anti-parallel beta sheets are usually connected with turns O d. Side chains of residues are alternated above and below the sheet a.
Draw a parallel beta sheet and an antiparallel beta sheet (three strands each). Show the hydrogen bonding pattern as well as the positions of the R groups of the amino acids. You do not need to draw the exact atoms; a simple representation is fine.
Classify each peptide chain as part of a parallel β sheet, part of an antiparallel β sheet, either type of β sheet, or not part of a β sheet. Parallel β sheet // Antiparallel β sheet // Either // Neither
The amino acid shown below has an ionizable side chain with a pka of 4. When this amino acid is in a more basic solution (i.e., pH 11), it would resemble ionization state C and have a charge of -1 HO OH NH₂ lonization state A NH3 lonization state C HO OH NH3+ Ionization state B dyb NH₂ lonization state D
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
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.
A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial hydrolysis. From this information, deduce the primary structure of this polypep- tide. Fragments are grouped according to size. Pentapeptide Fragments Tetrapeptide Fragments Phe-Val-Asn-Gln-His Gln-His-Leu-Cys His-Leu-Cys-Gly-Ser His-Leu-Val-Glu Gly-Ser-His-Leu-Val Leu-Val-Glu-Ala
Select the correct statement about β-sheets: They have side chains exposed on one side of the sheet. They often exhibit a right-handed twist when viewed along their polypeptide strands. The torsion angles are identical in both parallel and antiparallel β-sheets. They are held together by disulfide bonds. They are associations of α-helical segments lying side by side.
Draw beta sheet with backbone hydrogen bonds, is this structure on the interior or exterior of the protein and why? Region 1: -Ser-Thr-Glu-His- Region 2: -Asp-Tyr-Lys-Asn
Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (c) Outline how you would investigate whether BCMAP would be an effective inhibitor for the protein in competition with the molecules that the protein normally targets, and any solvent. Figure 1. 4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and brown, respectively) in the active site of the protein structure.
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
Name the protein structural element shown in yellow in the figure: B-barrel reverse turn disordered region a-helix parallel ß sheet