6) Proline is not commonly found in the middle of a-helices because its ring structure prevents it fromadopting the proper value and because it disrupts the hydrogen-bonding pattern of the helix. Lookingat the structure of proline in the amino acid sequence below, suggest how this residue would disrupt thehydrogen-bondingpattern of an a-helix.'NHRNNH***R

A protein's function depends on its structure. There are four levels of protein structure: primary,…

Answered: 6) Proline is not commonly found in the…

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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The diagram to the right illustrates the inter-actions of the amino acid side chains of two a-helical polypeptide strands in a coiled-coil, viewed end-on and projected along the helix axes from the N-terminal to the 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? f C b g e d a' a d' g b' f'
Given the polypeptide chain below: Ala-Arg-Val-His-Asp-Gln 1. What is the N-terminus? 2.What is the C-terminus?
An a helix would be destabilized MOST by ○ a glycine residue adopting alpha-helical backbone dihedral angles ○ interactions between neighboring Asp and Arg residues ○ interactions between two adjacent hydrophobic Val residues O the presence of an Arg residue near the carboxyl terminus of the a helix O the presence of two Lys residues near the amino terminus of the a helix
Proline 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.
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.
1) what is the net charge of the amino acid leucine of it is on the C-terminus end and why? 2) if the amino acid was changed to lysine on the c-terminus end explain why and what the net charge would be?.
Figure 1 shows the structure of adenine and thymine. (i) (ii) NH adenine C-H thymine Figure 1 Illustrate the potential tautomers of adenine and thymine. Draw a chemical structure of Thyminc-Adenine (T-A) base pair and label the patterns of hydrogen bond acceptors, donors in the major groove of the TA base pair.
3) You are working on a protein with the following sequence in an area of interest. -Asp-Leu-Leu-Gln-Glu-Glu-Asp-Glu-Ser-Arg a. The current structure, solved at pH 7.4, of this segment has an alpha helix that is disrupted a er the Gln. Why might the alpha helix stop at this residue? b. This protein is involved in Lysosomes in vivo. The secondary structure of this region is expected to change into a complete alpha helix. Why might this change into a complete helix? ( Hint: Lysosomes are acidic!)
The amino acids leucine and threonine in general tolerate being in an alpha helix. However having too many of these residues close together may disrupt an alpha helix. Why do you think this occurs?
The primary amino acid sequence of a stretch of polypeptide is Asp-Glu-Pro-Lys-His-Arg. Would you expect this portion of the polypeptide to form an alpha helix at pH=5? Provide 3 reasons to justify your answer.
Estimate the length, in nm, of the four identical beta-strands drawn in blue in panel (B) of the image below, if they consists of only the amino residues of the two alpha-helices highlighted in purple in panel (A) of the image below. Assume that the amino acid residues of the two alpha-helices combined were folded in four beta-strands of identical length.
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

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