Abstract
AbstractThe 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 IO‐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‐lβ, the complex of calmodulin with a target peptide, and the specific complex of the transcription factor GATA‐1 with its cognate DNA target site.
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Dates
Type | When |
---|---|
Created | 15 years, 1 month ago (July 12, 2010, 1:21 a.m.) |
Deposited | 1 year, 10 months ago (Oct. 24, 2023, 8:06 a.m.) |
Indexed | 1 month, 3 weeks ago (July 2, 2025, 2:47 p.m.) |
Issued | 31 years, 5 months ago (March 1, 1994) |
Published | 31 years, 5 months ago (March 1, 1994) |
Published Online | 16 years, 7 months ago (Dec. 31, 2008) |
Published Print | 31 years, 5 months ago (March 1, 1994) |
@article{Clore_1994, title={Structures of larger proteins, protein‐ligand and protein‐DNA complexes by multidimensional heteronuclear NMR}, volume={3}, ISSN={1469-896X}, url={http://dx.doi.org/10.1002/pro.5560030302}, DOI={10.1002/pro.5560030302}, number={3}, journal={Protein Science}, publisher={Wiley}, author={Clore, G. Marius and Gronenborn, Angela M.}, year={1994}, month=mar, pages={372–390} }