Fast-time scale dynamics of outer membrane protein A by extended model-free analysis of NMR relaxation data
- 28 February 2010
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Biomembranes
- Vol. 1798 (2) , 68-76
- https://doi.org/10.1016/j.bbamem.2009.07.022
Abstract
No abstract availableKeywords
Funding Information
- NIH (GM51329)
This publication has 37 references indexed in Scilit:
- Solution State NMR Structure and Dynamics of KpOmpA, a 210 Residue Transmembrane Domain Possessing a High Potential for Immunological ApplicationsJournal of Molecular Biology, 2009
- Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spacesJournal of Biomolecular NMR, 2007
- Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensorJournal of Biomolecular NMR, 2007
- Probing the Flexibility of the DsbA Oxidoreductase from Vibrio cholerae—a 15N - 1H Heteronuclear NMR Relaxation Analysis of Oxidized and Reduced Forms of DsbAJournal of Molecular Biology, 2007
- Increasing the Accuracy of Solution NMR Structures of Membrane Proteins by Application of Residual Dipolar Couplings. High-Resolution Structure of Outer Membrane Protein AJournal of the American Chemical Society, 2006
- Fast Time Scale Dynamics of Protein Backbones: NMR Relaxation Methods, Applications, and Functional ConsequencesChemical Reviews, 2006
- Membrane Protein Dynamics versus Environment: Simulations of OmpA in a Micelle and in a BilayerJournal of Molecular Biology, 2003
- High-resolution structure of the OmpA membrane domainJournal of Molecular Biology, 2000
- Backbone Dynamics of Ribonuclease HI: Correlations with Structure and Function in an Active EnzymeJournal of Molecular Biology, 1995
- Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteinsJournal of the American Chemical Society, 1990