Premium
Conformation and dynamics of fibrous and membrane proteins as revealed by high‐resolution solid‐state nuclear magnetic resonance
Author(s) -
Saitǒ Hazime,
Tuzi Satoru,
Nishimura Katsuyuki,
Fukutani Akira,
Naito Akira
Publication year - 1996
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.19961010109
Subject(s) - solid state nuclear magnetic resonance , high resolution , relaxation (psychology) , nuclear magnetic resonance , resolution (logic) , chemical shift , membrane , dynamics (music) , nuclear magnetic resonance spectroscopy , chemistry , solid state , chemical physics , materials science , crystallography , physics , psychology , social psychology , biochemistry , remote sensing , artificial intelligence , computer science , acoustics , geology
We examined conformation and dynamics of a variety of fibrous and membrane proteins by means of the conformation‐dependent displacements of 13 C nuclear magnetic resonance (NMR) chemical shifts and their relaxation parameters, respectively, as recorded by high‐resolution solid‐state 13 C NMR. Determination of three‐dimensional structure of atomic resolution is also briefly described for a simple peptide on the basis of precise measurements of interatomic distances.