Pressure-dependent Changes in the Solution Structure of Hen Egg-white Lysozyme
- 1 April 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 327 (4) , 857-865
- https://doi.org/10.1016/s0022-2836(03)00209-2
Abstract
No abstract availableKeywords
Funding Information
- Biotechnology and Biological Sciences Research Council
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 37 references indexed in Scilit:
- Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR 1 1Edited by P. E. WrightJournal of Molecular Biology, 2002
- Low-Lying Excited States of Proteins Revealed from Nonlinear Pressure Shifts in 1H and 15N NMRBiochemistry, 2001
- The Protein Data BankNucleic Acids Research, 2000
- Pressure-induced changes in the folded structure of lysozymeJournal of Molecular Biology, 1997
- The Impact of Direct Refinement against Proton Chemical Shifts on Protein Structure Determination by NMRJournal of Magnetic Resonance, Series B, 1995
- The Volume of Atoms on the Protein Surface: Calculated from Simulation, using Voronoi PolyhedraJournal of Molecular Biology, 1995
- Application of 1H NMR chemical shifts to measure the quality of protein structuresJournal of Molecular Biology, 1995
- Thermal expansion of hen egg-white lysozyme: Comparison of the 1·9 Å resolution structures of the tetragonal form of the enzyme at 100 K and 298 KJournal of Molecular Biology, 1994
- Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheresJournal of Molecular Biology, 1987
- The hinge-bending mode in lysozymeNature, 1976