Using NMR-Detected Backbone Amide 1H Exchange to Assess Macromolecular Crowding Effects on Globular-Protein Stability
Authors:
- Andrew C. MiklosAMAndrew C. Miklos
- Conggang LiCLConggang Li
- Gary J. PielakGPGary J. Pielak
- 1 January 2009
- book chapter
- Published by Elsevier
- Vol. 466, 1-18
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Origin of the change in solvation enthalpy of the peptide group when neighboring peptide groups are addedProceedings of the National Academy of Sciences, 2009
- Using NMR to Distinguish Viscosity Effects from Nonspecific Protein Binding under Crowded ConditionsJournal of the American Chemical Society, 2009
- Protein Nuclear Magnetic Resonance under Physiological ConditionsBiochemistry, 2008
- Guiding Protein Aggregation with Macromolecular CrowdingBiochemistry, 2008
- Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological ConsequencesAnnual Review of Biophysics, 2008
- Residue-Level Interrogation of Macromolecular Crowding Effects on Protein StabilityJournal of the American Chemical Society, 2008
- Molecular crowding enhances native structure and stability of α/β protein flavodoxinProceedings of the National Academy of Sciences, 2007
- Projection−Reconstruction of Three-Dimensional NMR SpectraJournal of the American Chemical Society, 2003
- A novel application of nuclear Overhauser enhancement (NOE) in proteins: Analysis of correlated events in the exchange of internal labile protonsBiochemical and Biophysical Research Communications, 1980
- A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric studyJournal of Molecular Biology, 1974