Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. paramagnetic relaxation enhancement by nitroxide spin labels
Open Access
- 1 April 1997
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 268 (1) , 158-169
- https://doi.org/10.1006/jmbi.1997.0954
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. distance restraints from paramagnetic relaxation and calculation of an ensemble of structuresJournal of Molecular Biology, 1997
- Chemically crosslinked protein dimers: Stability and denaturation effectsProtein Science, 1995
- Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured stateBiochemistry, 1992
- DENATURED STATES OF PROTEINSAnnual Review of Biochemistry, 1991
- [5] Spin labeling of proteinsPublished by Elsevier ,1989
- Generation and evaluation of isotropic ESR spectrum simulationsJournal of Magnetic Resonance (1969), 1988
- Two-dimensional proton NMR of three spin-labeled derivatives of bovine pancreatic trypsin inhibitorBiochemistry, 1986
- Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopyChemical Physics Letters, 1980
- Spatial Configuration of Macromolecular ChainsScience, 1975
- Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance ExperimentsPhysical Review B, 1954