α-Keratin is an intermediate filament with a basic structural unit of two a helices in a coiled coil. Each helix has a seven-residuerepeating unit (heptad repeat). A representation of the a helices of a coiled coil dimer is shown. Each letter represents a differentamino acid residue.fgdeReview the table of amino acids.adgfIdentify the three true statements about the structure of keratin.☐ The a helix of the coiled coil is wound less tightly than predicted for an α helix.☐ Each polypeptide in the dimer has 3.6 residues per turn, and a nonpolar group occurs every 3.5 residues, resulting in aslight winding, or twist, around the other polypeptide, forming a coiled coil.Arg-Ala-His-Glu-His-Thr-Asp is a likely repeat in the a helix of keratin.☐ Val-Thr-Asp-Ala-Glu-Arg-His is a likely repeat in the a helix of keratin.☐ The residues at positions b and c are less likely to be polar or charged because they are in contact with the solvent.☐ Keratin molecules are very strong due to hydrophilic interactions between charged amino acid side chains.

Three True Statements About Keratin Structure : The α helix of the coiled coil is wound less tightly…

Answered: α-Keratin is an intermediate filament…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Similar questions

Among these amino acid combinations listed above, only the combination of Lys and Glu have side chains with groups that have the greatest ability to stabilize the tertiary structure of a protein. Explain by drawing (a) why Lys and Glu side chain interaction stabilizes the tertiary structure of a protein (b) why the pairs of Glu and Asp & Arg and Pro cannot provide the stability to the protein structure.
Together, these monomers make up what type of polymer (macromolecule)? List at least three (broad) functions that these macromolecules can perform. What is an example protein that we’ve discussed that uses of these functions? Using R as the side chain, draw the basic structure of an amino acid.
Draw the chair conformation of the whole of O-linked oligosaccharide pictured below, including the amino acid it is attached to.
Identify and encircle the peptide bonds in this polypeptide (Ala-Leu-Glu-Ala-Asn-Asp-Arg-Ala)?
A cytosolic protein has an important alpha amino group. The pKa of this group is approximately 8 when exposed to water outside of a protein. 1. What would happen to the pKa if this group was instead buried in the hydrophobic interior of the protein? Explain. 2. Let’s say in the hydrophobic interior of the protein, the group forms an ionic bond with a carboxylate group of the side chain of a charged Asparagine residue. How would the pKa of this alpha amino group compare with the pKa of the alpha amino group in the hydrophobic interior of the protein without a nearby Asparagine residue to form this ionic bond? Explain.
draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 put the name of each part and the charge pls then compute for the isoelectric point please show complete solution DEHINS
Of the 20 protein-derived amino acids shown in Table 27.1, which contain Q.) no chiral center
Assume you have a long polypeptide chain of Gly-Val dipeptides linked end to end. Explain the likely tertiary structure of this polypeptide chain. For example, is the chain likely to form an alpha helix, a beta sheet, or some other structure? Is the structure likely to display lots of folding, or very little folding? Can you make any other predictions about the tertiary structure? Explain your reasoning in a well-developed paragraph.
Write the peptides of the full name " RYJO NNALAMBA" Every symbol of the Fullname writes the expanded structure in a zwitterion form. Then give the name of the polypeptide as a single molecule of the full name
A schematic diagram of the helical structure of cytochrome b562 is reproduced below. Thisprotein belongs to the family of -proteins that have a four-helix bundle. Number the helices 1 – 4according to their N  C direction. Indicate relative orientations of the macrodipoles of helices 1 – 4adjacent to the diagram of cytochrome b562. Remember that according to the definition of a dipolethat the arrow points towards the positive end.
Given below is a sequence of a polypeptide: AVLLRKIFWFDLAG The pKas of different groups/side chains are shown in the table below: Group/side chain pka C-terminus 3.5 Asp 3.9 Glu 4.1 His 6.0 Cys 8.4 Tyr 10.5 Lys 10.5 Arg 12.5 N-terminus 9.0 What is the total charge of this molecule at pH 11? [ Select ] What is the total charge of this molecule at pH 13? [ Select ] What is the isolectric point for this molecule? (Select]
"Potassium Bromate (KBr03) is added to flour as a softener that strengthens the texture of bread. It can do this by forming disulfide bonds between two cysteine amino acids in a reaction similar to the chemical equation given below. The function of KBr03 is to remove the 2 electrons needed to form the disulfide bond as shown in the figure below. Each of the cysteine amino acids will be in a protein chain, so the reaction binds the two chains together, giving the dough cohesion. However, potassium bromate is a proven carcinogen and is only allowed in foods in the United States because bakers will add the right amount and correct It has been assumed to meet the temperature and cooking time conditions. " KBRO, + C,H¸NO,SH → KBr + H,O+C,H„N,O,S, Balance the reaction of potassium bromate (KBr03) with the cysteine molecule (C3H6 NO2 SH) by converting it into the reduced step matrix using the additive matrix method. (Kis the symbol of potassium in the question) (Homogeneous linear equation…

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