Assessing potential bias in the determination of rotational correlation times of proteins by NMR relaxation
- 1 January 1999
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 13 (2) , 101-112
- https://doi.org/10.1023/a:1008304220445
Abstract
The various factors that influence the reliable and efficient determination of the correlation time describing molecular reorientation of proteins by NMR relaxation methods are examined. Nuclear...Keywords
This publication has 20 references indexed in Scilit:
- Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domainNature Structural & Molecular Biology, 1998
- Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13Cα nuclear spin relaxationJournal of Biomolecular NMR, 1997
- Measurement of 13C?-13CO cross-relaxation rates in 15N-/13C-labelled proteinsJournal of Biomolecular NMR, 1996
- Study of protein dynamics in solution by measurement of 13C?-13CO NOE and 13CO longitudinal relaxationJournal of Biomolecular NMR, 1996
- Internal Mobility in the Partially Folded DNA Binding and Dimerization Domains of GAL4: NMR Analysis of the N−H Spectral Density FunctionsBiochemistry, 1996
- Internal Dynamics of Human Ubiquitin Revealed by 13C-Relaxation Studies of Randomly Fractionally Labeled ProteinBiochemistry, 1996
- Structural Determinants of Protein Dynamics: Analysis of 15N NMR Relaxation Measurements for Main-Chain and Side-Chain Nuclei of Hen Egg White LysozymeBiochemistry, 1995
- Backbone Dynamics of a Free and a Phosphopeptide-Complexed Src Homology 2 Domain Studied by 15N NMR RelaxationBiochemistry, 1994
- The Energy Landscapes and Motions of ProteinsScience, 1991
- Two-dimensional proton NMR study of human ubiquitin: a main chain directed assignment and structure analysisBiochemistry, 1987