Using Amide 1H and 15N Transverse Relaxation To Detect Millisecond Time-Scale Motions in Perdeuterated Proteins: Application to HIV-1 Protease
- 24 September 1998
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 120 (40) , 10534-10542
- https://doi.org/10.1021/ja981546c
Abstract
No abstract availableThis publication has 38 references indexed in Scilit:
- Measurement ofJand Dipolar Couplings from Simplified Two-Dimensional NMR SpectraJournal of Magnetic Resonance, 1998
- Three‐dimensional solution structure of the HIV‐1 protease complexed with DMP323, a novel cyclic urea‐type inhibitor, determined by nuclear magnetic resonance spectroscopyProtein Science, 1996
- Monitoring Macromolecular Motions on Microsecond to Millisecond Time Scales by R1ρ−R1 Constant Relaxation Time NMR SpectroscopyJournal of the American Chemical Society, 1996
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Secondary structure and signal assignments of human‐immunodeficiency‐virus‐1 protease complexed to a novel, structure‐based inhibitorEuropean Journal of Biochemistry, 1994
- Conformational backbone dynamics of the cyclic decapeptide antamanide. Application of a new multiconformational search algorithm based on NMR dataBiochemistry, 1993
- Dynamic properties of proteins from NMR spectroscopyCurrent Opinion in Biotechnology, 1993
- Chiral β and random fractional deuteration for the determination of protein sidechain conformation by NMRFEBS Letters, 1987
- Photoelectric Effects in the Silver HalidesPhysical Review B, 1966
- Spin—Echo NMR Studies of Chemical Exchange. I. Some General AspectsThe Journal of Chemical Physics, 1964