NMR structural studies of glutathione S-transferase.
NMR structural studies of glutathione S-transferase.
Related Articles NMR structural studies of glutathione S-transferase. Cell Mol Life Sci. 1998 Apr;54(4):359-62 Authors: Lian LY The use of nuclear magnetic resonance (NMR) spectroscopy for the structure determination of small proteins is now widely recognized; what is less frequently reported is the application of NMR techniques for high-resolution studies of large proteins (M(r) larger than 30 kD). We demonstrate here how an integrated approach, using heteronuclear NMR and X-ray crystallography, can provide useful and biologically important information for large protein systems. The dynamic features of the human Al-1 glutathione S-transferase and the role of the C-terminal region are being probed by NMR; in the X-ray crystal structure, the electron densities for this region of the protein are uninterpretable. PMID: 9614973 [PubMed - indexed for MEDLINE] Source: PubMed |
All times are GMT. The time now is 09:18 AM. |
Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Search Engine Friendly URLs by vBSEO 3.6.0
Copyright, BioNMR.com, 2003-2013