| Literature DB >> 8019409 |
Abstract
The recent development of a whole panoply of multidimensional heteronuclear-edited and -filtered NMR experiments has revolutionized the field of protein structure determination by NMR, making it possible to extend the methodology from the 10-kDa limit of conventional 2-dimensional NMR to systems up to potentially 35-40 kDa. The basic strategy for solving 3-dimensional structures of larger proteins and protein-ligand complexes in solution using 3- and 4-dimensional NMR spectroscopy is summarized, and the power of these methods is illustrated using 3 examples: interleukin-1 beta, the complex of calmodulin with a target peptide, and the specific complex of the transcription factor GATA-1 with its cognate DNA target site.Entities:
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Year: 1994 PMID: 8019409 PMCID: PMC2142707 DOI: 10.1002/pro.5560030302
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725