Match each of the statements below with the fibrous protein that mostly fits the description.Coiled-coil of alpha helicesV [ Choose]CollagenSilk fibroinKeratinTriple helical arrangement of polypeptidechainsExtended anti-parallel beta sheets[ Choose ]Characterized by a predominant (GSGAGA)nrepeat in the primary seguence[ Choose]Found in hair, feathers, scales, and nails[ Choose ]Is produced by insects and spiders[ Choose ]The sequence Gly-Pro-Hyp occursfrequently in this fibrous protein[ Choose ]Is characterized by the heptad pseudo-[ Choose ]repeatMajor component of skin, tendons,ligaments and teeth[ Choose ]Characterized by regular inter-sheet spacing[ Choose ]of 0.35 and 0.57 nm

Triple helix : Has three strands which have the same axis and differ in translation along axis.

Answered: V[Choose ] Collagen Coiled-coil of…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Estimate the number of amino acid residues in each of the two helices of a segment of the alpha-keratin coiled coil that is 23 nm long.
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?
You analyze a protein of 100 kDa using SDS-PAGE in the absence and presence of �-mercaptoethanol (BME) and observe the following band pattern in the gels: Which of the following statements about the protein is correct? (the image is attached) a. The protein consists of three polypeptide chains, two of which are connected via S-S bridges. b. The protein consists of two different polypeptide chains connected via S-S bridges. c. The protein has two different folding conformations. d. The protein consists of two different polypeptide chains linked to each other via non-covalent interactions.
using examples, discuss the classification of proteins into fibrous and globular classification. - I would want to use myoglobin as an example of glubular but I don't know if that falls in the category for fibrous
Both α-keratin and collagen are examples of fibrous proteins. What is a fibrous protein? In 4-6 sentences, compare and contrast the structures of α-keratin and collagen. A)Will have the greatest absorbance at 280 nm B)Is the most negatively charged at pH7 C)Is the most positively charged at pH7
Which intermolecular forces are important in acetic acid, CH3 –(C=0)-oh? A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain. The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.
Compute for the albumin to globulin (A/G) ratio using these data given Albumin= 51.9g/L Total protein = 75.5 g/L Note: answer should be in ratio form
Consider protein folding that results when the following components interact: Where the solution is at a pH of 7, green (thick-dotted line) represents aspartic acid (R group contains a carboxylic acid with pKa = 4), orange (thick-solid line) represents lysine (R group contains an amine with pKa = 10), and blue (thin-solid line) represents hydrophilic groups. Rank the three complexes in order from lowest to highest dissociation constants Kd (low Kd values correspond to good binding constants and low energy, while high Kd values correspond to low binding constants and high energy) as determined by intermolecular charge-charge interactions. For those complexes with charge-charge interactions being equal, look at the possibility for the formation of hydrogen bonds via carboxylic acid dimers (only possible when the carboxylic acid is protonated) which are low energy structures.
Transmembrane portrudes on both sides. Integral protein is in the width of the bilayer and may portrude on one or both sides of the bilayer. Is Transmembrane Protein semi-similar to Integral Proteins? How can we tell the difference of the two?
What molecule allowed our target protein to elute off our affinity column? O a. lysozyme O b. BSA O c. imidazole O d. Laemmli O e. PMSF What information can isoelectric focusing provide about a protein? choose one or more: a. its pl b. its degree of purity c. its Km d. its molecular weight
Glycophorin is an integral membrane protein found on the surface of red blood cells that is important for binding to the malaria parasite. Name three different amino acids that you might expect to be present in the region of this protein that spans the lipid bilayer and name three different amino acids that you would expect to be absent from this region. For each group, describe what those amino acids have in common that distinguishes them from the other group.
Both a-keratin and collagen are fibrous proteins.however,the hydrogen bonding pattern is different between the helices of the respective proteins.what os the major difference?

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V[Choose ] Collagen Coiled-coil of alpha helices Silk fibroin Keratin Triple helical arrangement of polypeptide chains