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Proton—proton Overhauser NMR spectroscopy with polypeptide chains in large structures.

Proton—proton Overhauser NMR spectroscopy with polypeptide chains in large structures.

Authors :
Horst, Reto
Wider, Gerhard
Fiaux, Jocelyne
Bertelsen, Eric B.
Horwich, Arthur L.
Wüthrich, Kurt
Source :
Proceedings of the National Academy of Sciences of the United States of America. 10/17/2006, Vol. 103 Issue 42, p15445-15450. 6p. 4 Graphs.
Publication Year :
2006

Abstract

The use of ¹H-¹H nuclear Overhauser effects (NOE) for structural studies of uniformly deuterated polypeptide chains in large structures is investigated by model calculations and NMR experiments. Detailed analysis of the evolution of the magnetization during ¹H-¹H NOE experiments under slow-motion conditions shows that the maximal ¹H-¹H NOE transfer is independent of the overall rotational correlation time, even in the presence of chemical exchange with the bulk water, provided that the mixing time is adjusted for the size of the structure studied. ¹H-¹H NOE buildup measurements were performed for the 472-kDa complex of the 72-kDa cochaperonin GroES with a 400-kDa single-ring variant of the chaperonin GroEL (SR1). These experiments demonstrate that multidimensional NOESY experiments with cross-correlated relaxation-enhanced polarization transfer and transverse relaxation-optimized spectroscopy elements can be applied to structures of molecular masses up to several hundred kilodaltabs, which opens new possibilities for studying functional interactions in large maromolecular assemblies in solution. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00278424
Volume :
103
Issue :
42
Database :
Academic Search Index
Journal :
Proceedings of the National Academy of Sciences of the United States of America
Publication Type :
Academic Journal
Accession number :
23013933
Full Text :
https://doi.org/10.1073/pnas.0607141103