Structures of larger proteins in solution: Three- and four-dimensional heteronuclear NMR spectroscopy

Conference · Thu Dec 01 04:00:00 EST 1994

OSTI ID:83376

Gronenborn, A M; Clore, G M ^[1]

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1. National Institutes of Health, Bethesda, MD (United States)

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.

• Research Organization: Los Alamos National Lab., NM (United States)
• OSTI ID: 83376
• Report Number(s): LA--12893-C; CONF-9403228--; ON: DE95012795
• Country of Publication: United States
• Language: English

Related Subjects

40 CHEMISTRY
55 BIOLOGY AND MEDICINE
BASIC STUDIES
DYNAMIC FUNCTION STUDIES
ISOTOPE APPLICATIONS
MOLECULAR STRUCTURE
NMR IMAGING
NUCLEAR MAGNETIC RESONANCE
PROTEIN STRUCTURE
PROTEINS
X-RAY DIFFRACTION