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Helix change of polypeptides in the solid state as studied by NMR spectroscopy
Author(s) -
Ando Isao
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.19961010142
Subject(s) - solid state nuclear magnetic resonance , nuclear magnetic resonance spectroscopy , solid state , spectroscopy , characterization (materials science) , high resolution , crystallography , materials science , nuclear magnetic resonance spectroscopy of nucleic acids , chemistry , helix (gastropod) , resolution (logic) , transverse relaxation optimized spectroscopy , fluorine 19 nmr , nuclear magnetic resonance , stereochemistry , nanotechnology , physics , biology , ecology , remote sensing , quantum mechanics , artificial intelligence , geology , snail , computer science
The conformational characterization of solid polypeptides has been carried out by means of high‐resolution solid‐state NMR. It has been demonstrated that high‐resolution solid‐state NMR spectroscopy is a very useful means for elucidating the structure of polypeptides and proteins in the solid state.