High-Field 1H MAS and 15N CP-MAS NMR Studies of Alanine Tripeptides and Oligomers:  Distinction of Antiparallel and Parallel β-Sheet Structures and Two Crystallographically Independent Molecules

β-Strand peptides are known to assemble into either antiparallel (AP) or parallel (P) β-sheet forms which are very important motifs for protein folding and fibril formations occurring in silk fibroin or amyloid proteins. Well-resolved 1H NMR signals including NH protons were observed for alanine tri...

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Veröffentlicht in:	The journal of physical chemistry. B 2007-08, Vol.111 (30), p.9172-9178
Hauptverfasser:	Suzuki, Yu, Okonogi, Michi, Yamauchi, Kazuo, Kurosu, Hiromichi, Tansho, Masataka, Shimizu, Tadashi, Saitô, Hazime, Asakura, Tetsuo
Format:	Artikel
Sprache:	eng
Schlagworte:	Alanine - chemistry Algorithms Amyloid - chemistry Crystallography, X-Ray Magnetic Resonance Spectroscopy - instrumentation Magnetic Resonance Spectroscopy - methods Magnetics Molecular Structure Nitrogen Isotopes Peptides - chemistry Protein Folding Protein Structure, Secondary Protons
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