B-sheets exist only in fibrous proteins. The a-helix is stabilized by hydrogen bonds petween C=O and -NH- of the peptide packbone. The a-helix can be composed of more than one polypeptide chain.
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From the following statements, which is true?
![B-sheets exist only in fibrous proteins.
The a-helix is stabilized by hydrogen bonds
between C=O and -NH- of the peptide
backbone.
The a-helix can be composed of more than
one polypeptide chain.
The B-sheet is stabilized by ionic interactions
between the side chains of amino acids.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fbec26530-ad8e-474a-bebb-f27b71a5622d%2F516cd3e6-a4b6-421e-91d7-ebd8effb8b5b%2Fme2zxog_processed.jpeg&w=3840&q=75)
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- 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 TA 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-Ala1
- An a-Helix (or helices) is often found at anion binding sites of different proteins. Explain this observation using a schematic drawing of a-helix. Clearly indicate the direction of the dipole and the N-terminus of the helix. Show the structure of the functional group of the glutamic acid side chain in its (general) base form.Given the description of four different proteins above: Which protein will have the highest mobility in an SDS-PAGE gel?Which amino acid sequence will form part of which protein structure, and why? Sequence 1: Ser-Phe-Gln-Val-Lys-Leu-His-Tyr-Asp-Val Sequence 2: Glu-Tyr-Leu-Asn-Phe-Ala-Gln-Val-Leu-Arg __Amphipathic beta strand __ Amphipathic alpha helix
- 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 handedProline 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.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.
- Using a copy of a helical wheel (attached to the end) plot the amino acids of the helix on the helical wheel. Is there any evidence of the helix as a whole being amphipathic or having a “sidedness"? Explain yes or no. Are the amino acid side chains in close proximity of one another or staggered to minimize steric hinderance between side chains? Explain the pattern you observe.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 CysAssume that the 3 polypeptide strands shown below form a parallel B-sheet. Select amino acids AA1, AA2, and AA3 so that the parallel B-sheet is amphipathic and remains stable. Glu-lle-Asn-AA1-Cys-Val Ser-AA2-GIn-Leu-Lys-Phe Lys-Met-Cys-Leu-AA3-Val O AA1 = Pro, AA2 = Leu, AA3 = lle O AA1 = Val, AA2 = Leu, AA3 = Asn O AA1 = Ala, AA2 = Gly, AA3 = Leu AA1 = Phe, AA2 = Arg, AA3 = Ala O O