NMR exchange broadening arising from specific low affinity protein self-association: Analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1
- 1 January 1999
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 14 (4) , 307-320
- https://doi.org/10.1023/a:1008319917267
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Heteronuclear relaxation study of the PH domain of β-spectrin: restriction of loop motions upon binding inositol trisphosphate 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- Ca2+ Coordination to Backbone Carbonyl Oxygen Atoms in Calmodulin and Other EF-Hand Proteins: 15N Chemical Shifts as Probes for Monitoring Individual-Site Ca2+ CoordinationBiochemistry, 1998
- NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82AJournal of Molecular Biology, 1997
- The counterreceptor binding site of human CD2 exhibits an extended surface patch with multiple conformations fluctuating with millisecond to microsecond motionsProtein Science, 1997
- The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibrationJournal of Molecular Biology, 1997
- Contributions to Conformational Entropy Arising from Bond Vector Fluctuations Measured from NMR-Derived Order Parameters: Application to Protein FoldingJournal of Molecular Biology, 1996
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Backbone Dynamics of Ribonuclease HI: Correlations with Structure and Function in an Active EnzymeJournal of Molecular Biology, 1995
- Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5å resolutionStructure, 1994
- A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nucleaseBiochemistry, 1989