Abstract
Since the first experimental observation of nuclear magnetic resonance (NMR) in bulk matter more than 45 years ago (Bloch et al., 1946; Purcell et al., 1946), its history has been punctuated by a series of revolutionary advances that have greatly expanded its horizons. Indeed, methodological and instrumental developments witnessed over the past two decades have turned NMR into the most diverse spectroscopic tool currently available. Applications vary from exploration of natural resources and medical imaging to determination of the three-dimensional structure of biologically important macromolecules (Wüthrich, 1986; Kaptein et al., 1988; Bax, 1989; Clore and Gronenborn, 1989; Markley, 1989; Wüthrich, 1989; Wagner et al., 1992). The present chapter focuses primarily on the methodological advances in this latter application, particularly as they relate to the study of proteins in solution.
Adapted from Bax, A. and Grzesiek, S., Accounts of Chemical Research (in press).
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Bax, A., Grzesiek, S. (1993). Methodological Advances in Protein NMR. In: Clore, G.M., Gronenborn, A.M. (eds) NMR of Proteins. Topics in Molecular and Structural Biology. Palgrave, London. https://doi.org/10.1007/978-1-349-12749-8_2
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DOI: https://doi.org/10.1007/978-1-349-12749-8_2
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