Full length resilin that is not in a cell is thought by some to form a tertiary structure of this form (picture attached) The yellow portions represent exon 1 and the blue portions exon 3. These structures assemble into a kind of lattice or network.
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Full length resilin that is not in a cell is thought by some to form a tertiary structure of this form (picture attached)
The yellow portions represent exon 1 and the blue portions exon 3. These structures assemble into a kind of lattice or network. In full length resilin, stress in the form of mechanical pressure or heating to remove water results in a tighter network that excludes any water internally.
How might this behavior of resilin produce its ‘elasticity’? Explain how the looser water containing structure and the tighter water excluding structure may give us a mechanism for the elasticity.
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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.Bacteriorhodospin (Mw = 26 kDa) is a protein with purple colour. The protein acts as a light-activated proton pump that provides energy for cellular functions. The structure, revealed by both electron microscopy and X-ray crystallography, showed that the protein consists of 7 transmembrane spanning helices (TMH). Each TMH traverses the lipid bilayer completely (thickness of 45 Å). a)Calculate the minimum number of amino acid residues needed per TMH to completely cross the membrane. b)Estimate how large a fraction of the bacteriorhodopsin protein that is made up by TMHs. c)Now that you know the fraction of the protein that is made up by TMHs, at which ψ/φangles will the amino acids cluster in a Ramachandran plot?The dimensions of prokaryotic ribosomes are approximately 14 nm by 20 nm. If ribosomes occupy 20% of the volume of a bacterial cell, calculate how many ribosomes are in a typical cell as E. coli. Assume that the shape of a ribosome is approximately that of a cylinder.
- 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 phosphorylatedA group of membrane proteins can be extracted from membranes only by using detergents. All the proteins in this group have a similar amino acid sequence at their C-terminus: -KKKKKXXC (where K stands for lysine, X stands for any amino acid, and C stands for cysteine). This sequence is essential for their attachment to the membrane. What is the most likely way in which the C-terminal sequence attaches these proteins to the membrane? The cysteine residue is covalently attached to a membrane lipid. The peptide spans the membrane as an α helix. The peptide spans the membrane as part of a β sheet. The positively charged lysine residues interact with an acidic integral membrane protein.Specific rotation is a measure of a solution's capacity to rotate circularly polarized light. The unfolding of the α helix of a polypeptide to a randomly coiled conformation is accompanied by a large decrease in a property called specific rotation. Polyglutamate, a polypeptide made up of only l-Glu residues, is an α helix at pH 3. When researchers raise the pH to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (l-Lys residues) is an α helix at pH 10, but when researchers lower the pH to 7, the specific rotation also decreases, as shown in the graph. The graph plots pH on the horizontal axis ranging from 0 to 14, labeled in increments of 2, against specific rotation on the vertical axis. The curve for poly (Lys) begins as a horizontal line just above the horizontal axis. This is labeled, random conformation. At 8.5, it bends sharply upward and becomes diagonal at 8.8 until 9.9, when it reaches a height of two-thirds of the height of the…
- Which of the following statements are true? Electrostatic interactions are the dominant forces in protein molecular recognition. When two proteins form a complex there is an unfavorable loss of rotational-translational entropy. Protein-protein interfaces are most often dry. The exclusion of water results in an unfavorable loss in rotational-translational entropy. The free energy change associated with the formation of an enzyme-substrate complex almost always results in an unfavorable reduction in conformational entropy of the proteins. Burial of an uncompensated positive charge inside proteins is usually unfavorable. So-called van der Waals’ interactions are essentially electrostatic in origin. Steric complementarity of the two partners forming a complex is essential to achieve optimal free energy of binding. Structural models of proteins obtained from low temperature crystallography are excellent descriptions of all biochemically relevant aspects of their function.Pro-CHEMBIO peptide is a large peptide sequence with three disulfide bonds (indicated by the lines between cysteine residues). CHEMBIO Protease cleaves amide bonds between two basic amino acid residues to give the final peptide that is active in the body. The products of this protease reaction are: 1. Two chains that make up active CHEMBIO peptide, which contain the N- and C-terminus sections of the original Pro-CHEMBIO molecule 2. A separate inactive peptide What if instead of CHEMBIO Protease, this peptide was cleaved by trypsin? Indicate the cleavage locations on the structure below. asapChoose if it's true or false Different from RNA since in the latter the internucleotide linkages are between C-2’ and C-5’ A long chain polymer in which the internucleotide linkages are of the diester type between C-3’ and C-5’ Usually present in tissues as a nucleoprotein and cannot be separated from its protein component Hydrolyzed by weak alkali (pH 9 to 100°C)
- The answer given in problem 31. 17 is inadequate for me, and I simply don't understand the explanation for the answer... The problem is: Ribosoms were isolated from bacteria grown in a "heavy" medium (13C and 15N) and from bacteria grown in "light" medium (12C and 14N). These 70S ribosoms were added to an in vitro system engaged in protein synthesis. An aliquot removal serveral hours later was analyzed by density-gradient centrifugation. How many bands of 70S ribosoms would you expect to see in the density gradient? Is it possible to give a more comprehensive explanation? :)The unfolding of the α helix of a polypeptide to a randomly coiled conformation is accompanied by a large decrease in a property called specific rotation, a measure of a solution’s capacity to rotate circularly polarized light. Polyglutamate, a polypeptide made up of only L-Gluresidues, has the α-helix conformation at pH 3. When the pH is raised to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (L-Lys residues) is an α helix at pH 10, but when the pH is lowered to 7 the specific rotation also decreases, as shown by the following graph. What is the explanation for the effect of the pH changes on the conformations of poly(Glu) and poly(Lys)? Why does the transition occur over such a narrow range of pH?Using the the enzyme acid hydrolase in the lysosome: What is the final destination in which the protein will function? Which features will the protein receive during its manufacture? What is the primary structure (general)? Where is the primary structure made? Where are the secondary and tertiary structures made? Will the protein travel through any organelles during its manufacture? Which ones? What would be the overall result if some part of the manufacture process went wrong, such that the protein ended up as nonfunctional?