Comprehensive NOE characterization of a partially folded large fragment of staphylococcal nuclease Δ131Δ, using NMR methods with improved resolution
Open Access
- 12 September 1997
- journal article
- editorial
- Published by Elsevier in Journal of Molecular Biology
- Vol. 272 (1) , 9-20
- https://doi.org/10.1006/jmbi.1997.1219
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Comparison of the Backbone Dynamics of a Folded and an Unfolded SH3 Domain Existing in Equilibrium in Aqueous BufferBiochemistry, 1995
- Rules for α-Helix Termination by GlycineScience, 1994
- Unfolded proteins, compact states and molten globulesCurrent Opinion in Structural Biology, 1992
- Defining Solution Conformations of Small Linear PeptidesAnnual Review of Biophysics, 1991
- Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in bindingBiochemistry, 1991
- Proline isomerism leads to multiple folded conformations of calbindin D9k: direct evidence from two-dimensional 1H NMR spectroscopy.Proceedings of the National Academy of Sciences, 1989
- A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nucleaseBiochemistry, 1989
- Proline isomerism in staphylococcal nuclease characterized by NMR and site-directed mutagenesisNature, 1987
- Solvation energy in protein folding and bindingNature, 1986
- Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residuesBiochemistry, 1975