High Pressure NMR Reveals that Apomyoglobin is an Equilibrium Mixture from the Native to the Unfolded
- 1 July 2002
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 320 (2), 311-319
- https://doi.org/10.1016/s0022-2836(02)00449-7
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 48 references indexed in Scilit:
- High pressure NMR reveals a variety of fluctuating conformers in β-lactoglobulinJournal of Molecular Biology, 2001
- Pressure-resisting cell for high-pressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fieldsReview of Scientific Instruments, 2001
- The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by 1H NMRJournal of Molecular Biology, 2000
- Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobinJournal of Molecular Biology, 1999
- Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Structural Characterization of the Molten Globule and Native States of Apomyoglobin by Solution X-ray ScatteringJournal of Molecular Biology, 1995
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- The ‘molten globule’ state is involved in the translocation of proteins across membranes?FEBS Letters, 1988
- Thermodynamic study of the apomyoglobin structureJournal of Molecular Biology, 1988