V[Choose ] Collagen Coiled-coil of alpha helices Silk fibroin Keratin Triple helical arrangement of polypeptide chains
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- α‑Keratin is an intermediate filament with a basic structural unit of two α helices in a coiled coil. Each helix has a seven‑residue repeating unit (heptad repeat). A representation of the α helices of a coiled coil dimer is shown. Each letter represents a different amino acid residue.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?Create a ROUGH SKETCH (no need for exact hydropathy indices and residue numbers) of the hydropathy plot for the given membrane protein. -coo Please follow the color assignment of the helical domains and properly label the plot and axes. Here is an example: Amino Outside terminus Transmembrane helices are predicted by hydrophobic stretches of 20-25 aa residues 10 50 100 150 200 250 Hydrophobic Inside Hydrophilic Carboxyl terminus -3 10 50 100 150 200 250 Residue number Bacteriorhodopsin Hydropathy index
- The lipid portion of a typical bilayer is about 3 nm thick. (a) Calculate the number of residues in an a helix that will just span this distance. (b) The epidermal growth factor receptor has a single transmem- brane helix. Find it in this partial sequence: .--RGPKIPSIATGMVGALLLLVVALGIGILFMRRRH-…T/F Type I collagen fibers, that consist of collagen triple helices aligned side-by-side, are strengthened by covalent cross-links between amino acid side chains of different collagen triple helices. True O FailseRoughly sketch the hydropathy plot for the given hypothetical membrane protein. Follow the color assignment of the helical domains and properly label your plot and axes (NB: Only a rough sketch is being asked. No need be exact with the hydropathy indices and residue numbers). CO-
- 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?Here is a putative peptide sequence (position number on top of residues): 1 2 3 4 5 6 7 8 9 10 11 12 13 NH2- G C G N V T H N Q C V L S -COOH If expressed in a eukaryotic cell (please mark your answer in the blank space): Position(s) ___ could be N-glycosylated Position(s) ___ could be modified with myristic acid and the bond formed would be a ______________ Position(s) ______and _____ could be modified with palmiti c acid and the bond formed would be a ______________ Positio n(s) ________ could be a segment of a lipid-linked protein with a farnesyl anchor and the bond formed would be a ______________ Position(s) ________ could be a segment of an O-glycosylated protein Position(s) ________ could be modified with a glycosylphosphatidylinositol (GPI) anchor Position(s) ________ could be phosphorylatedBacteriorhodopsin is an integral membrane protein containing 248 amino acids. X- ray analysis of this protein reveals that it consists of seven parallel a-helical segments, each of which traverses the bacterial cell membrane. Calculate the minimum number of amino acid residues necessary for a single a-helical segment to completely traverse the bacterial cell membrane (assume the membrane has a thickness of 4.1 nm). (a) (b) Estimate the fraction of the bacteriorhodopsin protein that is involved in membrane-spanning helices.
- What could be the reason why hydroxylation of proline residues is critical to the structural integrity of collagen? Select the correct response The hydroxyl moities in Pro form disulfide bonds which stabilize collagen structure. The hydroxyl moities in Pro form ionic bonds (salt bridges) which stabilize collagen structure. The hydroxyl moities in Pro form hydrophobic interactions which stabilize collagen structure. The hydroxyl moities in Pro form peptide bonds which stabilize collagen structure. The hydroxyl moities in Pro form H-bonds which stabilize collagen structure.What is the length in AA’s of the LilP protein? Assume fMet is NOT CLEAVED. Write out the sequence of the polypeptide in AA: use the three letter notation, e.g. Met-Ser-Pro-How many alpha helices comprise this structure (2JHO-myoglobin)? Number the helices with helix 1 at the N-terminus.