Beta pleated sheet protein model

Study the beta-pleated sheet, a common secondary structure of proteins. Set includes sufficient components to make 15 peptide linkages. With instruction sheet. The secondary structure of silk is the beta pleated sheet. The primary structure of silk contains the amino acids of glycine, alanine, serine, in specific repeating pattern. These three amino acids make up 90% of the protein in silk. Once again, side chain interactions play a major role in allowing or disallowing such secondary structures to form. But in fact, most proteins do have extensive regions folded into alpha-helices and beta-pleated sheets. Secondary structure consists mostly of these 2 structures, the alpha helix and the beta-pleated sheet. Amyloid disease: visible protein deposits that can be stained. Plaques found in 10% of CJD, higher percentage in other TSEs. Two distinct forms, PrP-C and PrR-res. Membrane-bound protein, 254 amino acids, 2 glycosylation sites. Conserved between species, but with slight changes resulting in a disease species barrier 1. Figure 1.7 shows Phi/Psi angles measured from solved protein structures experimentally as well as values calculated by Ramachandran. For alpha-helical and β-sheet conformations, estimate by inspection of fig. 1.7 the deviation of the range limits between the experimental and calculated data sets. 2. Dzwolak W, Muraki T, Kato M, Taniguchi Y „Chain-length dependence of alpha-helix to beta-sheet transition in polylysine: model of protein aggregation studied by temperature-tuned FT-IR spectroscopy” Biopolymers, 73 (2004) 463-469,