Structural Characterization of Unfolded States of Apomyoglobin using Residual Dipolar Couplings
- 9 June 2004
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 340 (5) , 1131-1142
- https://doi.org/10.1016/j.jmb.2004.05.022
Abstract
No abstract availableKeywords
This publication has 63 references indexed in Scilit:
- Short-range, Long-range and Transition State Interactions in the Denatured State of ACBP from Residual Dipolar CouplingsJournal of Molecular Biology, 2004
- Intrinsic Disorder in Cell-signaling and Cancer-associated ProteinsJournal of Molecular Biology, 2002
- What is the average conformation of bacteriophage T4 lysozyme in solution? a domain orientation study using dipolar couplings measured by solution NMRJournal of Molecular Biology, 2001
- NMR characterization of residual structure in the denatured state of protein LJournal of Molecular Biology, 2000
- Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactionsNature Structural & Molecular Biology, 1998
- Measurement ofJand Dipolar Couplings from Simplified Two-Dimensional NMR SpectraJournal of Magnetic Resonance, 1998
- Two forms of the pH 4 folding intermediate of apomyoglobinJournal of Molecular Biology, 1998
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- 1H, 13C and 15N chemical shift referencing in biomolecular NMRJournal of Biomolecular NMR, 1995
- Thermodynamic study of the apomyoglobin structureJournal of Molecular Biology, 1988