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

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

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 improve...

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Veröffentlicht in:Current opinion in biotechnology 1995, Vol.6 (1), p.81-88
Hauptverfasser: Clowes, Robin T, Crawford, Arthur, Raine, Andrew RC, Smith, Brian O, Laue, Ernest D
Format: Artikel
Sprache:eng
Schlagworte:
Animals
Enzymes - chemistry
Magnetic Resonance Spectroscopy - methods
Protein Conformation
Protein Structure, Secondary
Proteins - chemistry
Sensitivity and Specificity
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Zusammenfassung: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 −270 amino acid residues).
ISSN:0958-1669
1879-0429
DOI:10.1016/0958-1669(95)80013-1