Supramolecular Antiparallel beta-Sheet Formation by Tetrapeptides Based on Amyloid Sequence This result indicates thatthe short peptide composed of aliphatic amino acid is capable of forminga β-sheet structure in the absence of aromatic amino acid andalso can mimic the function of the native amyloid...
R. Ghadiri.Beta-Sheet Peptide Architecture: Measuring the Relative Stability of Parallel vs. Antiparallel beta-Sheets. Angewandte Chemie . 1995K, Kobayashi,,J. R. Granja,,M. R. Ghadiri.β-Sheet Peptide Architecture: Measuring the Relative Stability of Parallel vs. Antiparallel β-Sheets. Angew...
Antiparallel Beta-Sheet refers to a common secondary structure in peptides/proteins where the structure exhibits a different orientation and symmetry compared to other structural elements such as alpha-helical structures. It is characterized by specific spectral features in SFG spectra and includes both ...
-sheet conformation of an acyclic cystine peptide The conformation of the acyclic biscystine peptide S,S-bis(Boc-Cys-Ala-OMe) has been studied in the solid state by x-ray diffraction, and in solution by1H-... PA Raj,SD Soni,N Ramasubbu,... - 《Biopolymers》 被引量: 8发表: 2010年...
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 ...
Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force MicroscopyThe aggregation of the intrinsically disordered protein alpha-synuclein (αS) into amyloid fibrils is thought to play a central role...
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...
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 ...
The effect of cooperative interactions between β-strands in enhancing β-sheet stability has been examined quantitatively by NMR using rationally designed synthetic peptides [β-hairpin (2β) and related 24-residue three-stranded antiparallel β-sheet (3β)] which are significantly folded in aqueous...
An intramolecular G-quadruplex structure with mixed parallel/antiparallel G-strands formed in the human BCL-2 promoter region in sol... Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. ...