Journal of Biomolecular NMR

, Volume 22, Issue 1, pp 1–8

Residual dipolar couplings: Synergy between NMR and structural genomics

Authors

    • Cellular Biochemistry and Biophysics ProgramMemorial Sloan-Kettering Cancer Center
  • Dinshaw J. Patel
    • Cellular Biochemistry and Biophysics ProgramMemorial Sloan-Kettering Cancer Center
Article

DOI: 10.1023/A:1013801714041

Cite this article as:
Al-Hashimi, H.M. & Patel, D.J. J Biomol NMR (2002) 22: 1. doi:10.1023/A:1013801714041

Abstract

Structural genomics is on a quest for the structure and function of a significant fraction of gene products. Current efforts are focusing on structure determination of single-domain proteins, which can readily be targeted by X-ray crystallography, NMR spectroscopy and computational homology modeling. However, comprehensive association of gene products with functions also requires systematic determination of more complex protein structures and other biomolecules participating in cellular processes such as nucleic acids, and characterization of biomolecular interactions and dynamics relevant to function. Such NMR investigations are becoming more feasible, not only due to recent advances in NMR methodology, but also because structural genomics is providing valuable structural information and new experimental and computational tools. The measurement of residual dipolar couplings in partially oriented systems and other new NMR methods will play an important role in this synergistic relationship between NMR and structural genomics. Both an expansion in the domain of NMR application, and important contributions to future structural genomics efforts can be anticipated.

dynamics and functionlong-range constraintsmulti-domain proteinsproteomicsRNA tertiary structure

Copyright information

© Kluwer Academic Publishers 2002