Protein dynamics: a study of the model-free analysis of NMR relaxation data
Authord'Auvergne, Edward J.
AffiliationSchool of Medicine: Biochemistry and Molecular Biology
Biochemistry and Molecular Biology
MetadataShow full item record
Document TypePhD thesis
Citationd'Auvergne, E. J. (2006). Protein dynamics: a study of the model-free analysis of NMR relaxation data, PhD thesis, Biochemistry and Molecular Biology, University of Melbourne.
Access StatusOpen Access
© 2006 Edward James d’Auvergne
The model-free analysis of NMR relaxation data, which is widely used for the study of protein dynamics, consists of the separation of the Brownian rotational diffusion from internal motions relative to the diffusion frame and the description of these internal motions by amplitude and timescale. Through parametric restriction and the addition of the Rex parameter a number of model-free models can be constructed. The model-free problem is often solved by initially estimating the diffusion tensor. The model-free models are then optimised and the best model is selected. Finally, the global model of all diffusion and model-free parameters is optimised. These steps are repeated until convergence. This thesis will investigate all aspects of the model-free data analysis chain. (For complete abstract open document)
KeywordsBrownian diffusion; data analysis; mathematical modelling; minimisation; model elimination; model selection; model-free analysis; NMR relaxation; optimisation; protein dynamics
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