Structures of larger proteins in solution: Three- and four-dimensional heteronuclear NMR spectroscopy (Conference) | OSTI.GOV
- ️Thu Dec 01 1994
OSTI.GOV Conference: Structures of larger proteins in solution: Three- and four-dimensional heteronuclear NMR spectroscopy
Conference · Thu Dec 01 05:00:00 UTC 1994
OSTI ID:83376
Complete understanding of a protein`s function and mechanism of action can only be achieved with a knowledge of its three-dimensional structure at atomic resolution. At present, there are two methods available for determining such structures. The first method, which has been established for many years, is x-ray diffraction of protein single crystals. The second method has blossomed only in the last 5 years and is based on the application of nuclear magnetic resonance (NMR) spectroscopy to proteins in solution. This review paper describes three- and four-dimensional NMR methods applied to protein structure determination and was adapted from Clore and Gronenborn. The review focuses on the underlying principals and practice of multidimensional NMR and the structural information obtained.
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Research Organization:
- Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
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OSTI ID:
- 83376
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Report Number(s):
- LA-12893-C; CONF-9403228-; ON: DE95012795; TRN: 95:004732-0007
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Resource Relation:
- Conference: Stable isotope applications in biomolecular structure and mechanisms, Santa Fe, NM (United States), 27-31 Mar 1994; Other Information: PBD: Dec 1994; Related Information: Is Part Of Stable isotope applications in biomolecular structure and mechanisms. A meeting to bring together producers and users of stable-isotope-labeled compounds to assess current and future needs; Trewhella, J.; Cross, T.A.; Unkefer, C.J. [eds.]; PB: 382 p.
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Country of Publication:
- United States
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Language:
- English