Improved methods for structural studies of proteins using nuclear magnetic resonance spectroscopy.

TitleImproved methods for structural studies of proteins using nuclear magnetic resonance spectroscopy.
Publication TypeJournal Article
Year of Publication1995
AuthorsClowes, RT, Crawford, A, Raine, AR, Smith, BO, Laue, ED
JournalCurr Opin Biotechnol
Volume6
Issue1
Pagination81-8
Date Published1995 Feb
ISSN0958-1669
KeywordsAnimals, Enzymes, Magnetic Resonance Spectroscopy, Protein Conformation, Protein Structure, Secondary, Proteins, Sensitivity and Specificity
Abstract

The past few years have seen the development of three- and four-dimensional heteronuclear nuclear magnetic resonance methods. Increased sophistication in labelling strategies, use of pulse-field gradients and the application of these methods at higher magnetic fields has, in combination with improved software, allowed studies of the structure, interactions and dynamics of significantly larger proteins (now up to approximately 270 amino acid residues).

DOI10.1016/0958-1669(95)80013-1
Alternate JournalCurr. Opin. Biotechnol.
Citation Key10.1016/0958-1669(95)80013-1
PubMed ID7894084