CommentsT140 has a rigidly structured conformation characterized by anantiparallel beta-sheetand a type II' beta-turn. A protuberance is formed on one side of the beta-sheet by the side-chain functional groups of the three amino acid residues (L-3-(2-naphthyl) alanine, Tyr5 and Arg14), ...
R. Beta-sheet peptide architecture: measuring the relative stability of parallel vs. antiparallel beta-sheets. Angew. Chem., Int. Ed. Engl. 1995, 34, 95-98.Kobayashi K, Granja JR, Ghadiri MR (1995) b-sheet peptide architecture: Measuring the relative stability of parallel vs antiparallel b...
Antiparallel {beta}-sheet architecture in Iowa-mutant {beta}-amyloid fibrils [Chemistry] Wild-type, full-length (40- and 42-residue) amyloid β-peptide (Aβ) fibrils have been shown by a variety of magnetic resonance techniques to contain cross-β structures in which the β-sheets have an ...
2009. Δ98Δ, a minimalist model of antiparallel β-sheet proteins based on intestinal fatty acid binding protein. Protein Sci. 18:735-746.Curto LM, Caramelo JJ, Franchini GR, Delfino JM. Delta 98 Delta, a minimalist model of antiparallel beta-sheet proteins based on intestinal fatty acid ...
Both these peptide molecules formed an antiparallel pleated β-sheet, and pseudo twofold symmetries existed in the repeated sequence. β-Turns formed at the fragments of d-Phe-Pro were classified into type II' based on their characteristics. The peptide conformations of TcGS and BzGS were ...
Balaram, Cystine peptides: The intra- molecular antiparallel L sheet conformation of a 20-membered cyclic peptide disul¢de, Biopolymers 26 (1987) 873^891.Kishore, R., S. Raghothama, and P. Balaram. 1987. Cystine peptides: the intramolecular antiparallel beta-sheet conformation of a 20-...
Matrix formulation of the transition from a statistical coil to an intramolecular antiparallel beta sheet. A tractible matrix formulation is developed for the formation of intramolecular antiparallel β sheets in a homopolymer chain molecule. The formulation is ... WL Mattice,HA Scheraga - 《...
Effects of side-chain orientation on the 13C chemical shifts of antiparallel beta-sheet model peptides. A.; Scheraga, H. A. Effects of Side-Chain Orientation on the 13C Chemical Shifts of Antiparallel β-sheet Model Peptides. J. Biomol. NMR 2007, ... ME Villegas,JA Vila,HA Scheraga ...
Studies the length-dependent stability and strand length limits in antiparallel beta-sheet secondary structure. Factors that determine native conformations of proteins; Possibility of an intrinsic limit to strand length for most sequences in antiparallel beta-sheet secondary structure; Use of designed pept...
Therefore, we suggest that a simple way to increase beta-hairpin stability, or the stability of an antiparallel edge strand, is to have a non-hydrogen bonded ring at the end of the strand. 展开 关键词: antiparallel/β‐bulge/β‐sheet/β‐turn/secondary structure ...