Study of Protein-H2O Interactions by Multidimensional NMR Spectroscopy
Abstract
Water has been shown to play an integral role in both structural and catalytic aspects of protein function. Strongly-bound water molecules are observed in high-resolution protein structures by x-ray diffraction studies of single crystals of protein molecules. The pilot studies described here were aimed at ascertaining the feasibility of detecting strongly-bound water molecules in solution using multidimensional heteronuclear NMR spectroscopy. 3D- (lH, 15N)-HMQC-ROESY spectroscopy was implemented on a Bruker AM-500 spectrometer and spectra were collected on a series of related HPr protein molecules. Interactions involving both H20 and -OH groups were reproducibly detected in the spectra. The results indicate that this approach is capable of yielding a limited amount of information concerning protein-water interactions and is not likely to become a generally-used technique.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 1993
- Accession Number
- ADA266955
Entities
People
- Rachel E. Klevit
Organizations
- University of Washington