Accession Number : ADA266955


Title :   Study of Protein-H2O Interactions by Multidimensional NMR Spectroscopy


Descriptive Note : Rept. 1 Apr 91-31 Mar 93,


Corporate Author : WASHINGTON UNIV SEATTLE DEPT OF BIOCHEMISTRY


Personal Author(s) : Klevit, Rachel E


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a266955.pdf


Report Date : Jul 1993


Pagination or Media Count : 8


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.


Descriptors :   *NUCLEAR MAGNETIC RESONANCE , *SPECTROSCOPY , *INTERACTIONS , *PROTEINS , *WATER , MOLECULES , INTEGRALS , X RAY DIFFRACTION , SINGLE CRYSTALS , HIGH RESOLUTION , HYDROGEN , THREE DIMENSIONAL , SPECTRA , BONDING , MOLECULAR STRUCTURE , CATALYSIS , PILOT STUDIES , SPECTROMETERS , AMINO ACIDS , HISTIDINE


Subject Categories : Biochemistry
      Inorganic Chemistry
      Physical Chemistry
      Atomic and Molecular Physics and Spectroscopy


Distribution Statement : APPROVED FOR PUBLIC RELEASE