The diagram to the right illustrates the inter-actions ofthe amino acid side chains of two a-helicalpolypeptide strands in a coiled-coil, viewed end-on andprojected along the helix axes from the N-terminal tothe C-terminal end. Are the macrodipoles of the two a-helices oriented parallel or anti-parallel? For this projec-tion is the positive end of the macro-dipole in the sur-face of the paper or below the surface?fCbgeda'a d'gb'f'

Coiled coils are super secondary structures formed as 2 or more alpha helices twist around each…

Answered: The diagram to the right illustrates…

Biology Today and Tomorrow without Physiology (MindTap Course List)

5th Edition

ISBN:9781305117396

Author:Cecie Starr, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Christine Evers, Lisa Starr

Chapter7: Gene Expression And Control

Section: Chapter Questions

Problem 2CT

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Shown below are two cartoon views of the small globular protein StrepG inwhich an α helix is packed against a four-strand β sheet. The sheet is madeup of two “β-hairpins” (a β-hairpin is a “β-turn-β” structure). Refer to theimages and answer the questions that follow: (a) Identify the locations of the N- and C-termini of StrepG.(b) Indicate the orientation of the helical macrodipole, showing the (δ+)and (δ-) ends of the macrodipole.(c) How many residues are in the helix?(d) Do you predict that the α helix and β sheet are amphiphilic or not?Briefly explain.(e) The following two peptides are part of the primary sequence of StrepG.Based on your answer to part (d), which one is more likely to correspondto the α helix? Which is most likely to be part of a β-hairpin? Explainyour choice.Peptide #1: DAATAEKVFKQYAND or Peptide #2: VDGEWTYDDATKTFTV
SYNZIPS are a-helices that can be used in synthetic biology to create coiled-coil interactions between two different proteins. SYNZIP1 is around 47 amino acids in length. If each turn in an a-helix is 3.6 residues in length and each turn is 5.4 Å in length, how long is SYNZIP1? Keep in mind that 1 Å = 10 nm. Present your answer in nm.
GLUT 1 contains several amphipathic transmembrane hellices, each with Its polar face oriented towards the central cavity, producing a transmembrane channel available for interaction with glucose, as shown in the figure below. Which of the following sequences are most likely to form a transmembrane helix? Helical wheel diagram is given for reference. a Ser-Ala-Val-Phe-Thr-lle-Met O Phe-Leu-Val-Thr-Asn-Met-lle O Val-Ser-Thr-Val-Phe-Asn-Glu Ser-Asn-Leu-Asp-Gin-lle-Phe O Asn-Leu-Ala-Ser-Gin-Phe-e
1. Consider the following α helix from myoglobin at pH 7. Gln-Gly-Ala-Met-Asn-Lys-Ala-Leu-Glu-His-Phe-Arg-Lys-Asp-Ile-Ala-Ala-Lys-Tyr(a) Label amino acids in the polypeptide above as follows: p for polar and uncharged, np for non polar, – for negatively charged, and + for positively charged.(b) How many complete turns are there in this helix?(b) Which side chains are likely to be on the side of the helix that faces the aqueous solvent? Why?(c) Which side chains are likely to face the interior of the protein? Why?
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.
The domain of a protien is approximately 350 residues in length. what is length (in A°) of this domain? if this same peptide segment were a true alpha helix, how long would it be? if the same segment were beta sheet, what would its length be?
Given the polypeptide chain below: Ala-Arg-Val-His-Asp-Gln 1. What is the N-terminus? 2.What is the C-terminus?
The predominant forms of actin inside a cell are ATP–G-actin and ADP–F-actin. Explain how the interconversion of the nucleotide state is coupled to the assembly and disassembly of actin subunits.
(c) The tube and cylinder diagram to the right illus- trates schematically the potassium channel protein from a bacterium. This channel protein consists of four identical polypeptide chains each comprised of 119 residues. The cyan ribbon illustrates only two of the polypeptide chains. The relative positions of 4 α-helices, one from each poly- peptide chain, are shown as cylinders. The red sphere in the central part of the diagram shows the position of a potas- sium ion identified by X-ray structure analysis. A cesium ion (green sphere) was also found to be stabilized in the same position when cesium chloride was introduced into the crys- tals. The cylinders each represent an α-helix running from Tyr62 to Thr74. Considering the position of the potassium ion, in- dicate on one of the cylinders at which end of the cylinder residue Tyr62 is found and at which end residue Thr74 is found. Explain the basis of your answer? Ala23 Thr119 (d) The N- and C-terminal residues of one of the…
To visualize the spatial arrangement of amino acid residues in an a-helix, it is helpful to imagine you are looking down the long axis of the helix, just as you would look down a soda straw. Viewed in this orientation, the residues form a circle, with each residue offset from its neighbor by 100 degrees. This representation is called a helical wheel. Use the circle below to indicate the position of each residue around the helix of the enzyme lysozyme. NH ...Arg - Cys - Glu- Leu - Ala Ala - Ala Met-Lys COO- The first two amino acids, Arg-1 and Cys-2, are shown as an example. Arg-1 O Glu-3 Which amino acid in the polypeptide is the first to pass the origin (i.e., which amino acid passes Arg- 1 first, completing one full circle)? Select the best answer. O Leu-4 O Ala-5 O Ala-6 O Ala-7 Met-8 O Lys-9 100° O none of the above Cys-2
In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe- Ser-Gin-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys The hydrophobic residues in this sequence are presented in boldface type. Use helix wheel to demonstrate this peptide is an amphipathic helix.
Alpha-helices have 3.6 amino acid residues per turn, ie a helix 36 amino acids long would form 10 turns, and The axial distance between adjacent residues is 3.5 Angstroms. Beta-helices have two residues per repeat unit which gives the beta-strand a 7 Angstrom pitch. This compares with the alpha-helix where the axial distance between adjacent residues is only 1.5 Angstroms. Then how many residues in an alpha-helix conformation would it take to traverse the same distance as 10 residues in beta-strand conformation?

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