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McMahon, Michael T.; Oldfield, Eric

doi:10.1023/a:1008339711590

Cited by 9 publications

(4 citation statements)

References 4 publications

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“…Practical aspects of data analysis, including model selection and error analysis, are not discussed herein. ,− In general, rotational diffusion tensors and generalized order parameters are reliably determined by NMR relaxation measurements. However τ e or τ s can be characterized precisely only over a relatively narrow range unless high quality data are available at multiple static magnetic field strengths.…”

Section: 3 Model-free Formalismmentioning

confidence: 99%

NMR Characterization of the Dynamics of Biomacromolecules

2004

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Section: 3 Model-free Formalismmentioning

confidence: 99%

NMR Characterization of the Dynamics of Biomacromolecules

2004

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“…Distinguishing between the various potential internal correlation functions is often reduced to detailed statistical analyses and requires a significant amount of relaxation data in order to be meaningful. Bayesian statistics appear to be particularly useful in this regard . Thus far, there are very few instances where the model-free treatment appears to give a qualitatively misleading view of the motion underlying relaxation.…”

Section: Describing the Motionmentioning

confidence: 99%

“…Bayesian statistics appear to be particularly useful in this regard. 67 Thus far, there are very few instances where the model-free treatment appears to give a qualitatively misleading view of the motion underlying relaxation.…”

Section: Model-free Form Of the Spectral Densitymentioning

confidence: 99%

Characterization of the Fast Dynamics of Protein Amino Acid Side Chains Using NMR Relaxation in Solution

2006

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A variety of technical issues such as the effects of macromolecular tumbling and the influence of competing relaxation mechanisms have also been largely resolved (vide infra). These advances have positioned solution NMR spectroscopy to efficiently and comprehensively characterize the fast internal dynamics of proteins of significant size. This review seeks to provide a compact but reasonably complete description of the theoretical and technical foundation for solution NMR relaxation methods that are currently being brought to bear on fast sub-nanosecond protein side chain dynamics and to present a summary of current findings and their possible significance. A survey of basic observations about side chain dynamics derived from NMR-relaxation studies is presented along with several analyses meant to dispel commonly held but apparently inaccurate correlations between dynamics, structure and function. How dynamics can enter into fundamental thermodynamic and kinetic aspects of protein function is also reviewed and illustrated with intriguing results from several systems that point to a promising future for this area of inquiry.

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“…243 proposed a protocol to determine iteratively the overall tumbling correlation time, even in the presence of large conformational exchange. Bayesian methods are also used for the determination of correlation times and order parameters [244].…”

Section: Describing the Relaxation Measurements In Terms Of Internal mentioning

confidence: 99%

Quantitative Analysis of Biomolecular NMR Spectra: A Prerequisite for the Determination of the Structure and Dynamics of Biomolecules

Malliavin

2006

COC

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Nuclear Magnetic Resonance (NMR) became during the two last decades an important method for biomolecular structure determination. NMR permits to study biomolecules in solution and gives access to the molecular flexibility at atomic level on a complete structure: in that respect, it is occupying a unique place i n structural biology. During the first years of its development, NMR was trying to meet the requirements previously defined in X-ray crystallography. But, NMR then started to determine its own criteria for the definition of a structure. Indeed, the atomic coordinates of an NMR structure are calculated using restraints on geometrical parameters (angles and distances) of the structure, which are only indirectly related to atom positions: in that respect, NMR and X-ray crystallography are very different. The indirect relation between the NMR measurements and the molecular structure and dynamics makes critical the precision and the interpretation of the NMR parameters and the development of quantitative analysis methods. The methods published since 1997 for liquid-NMR of proteins are reviewed here. First, methods for structure determination are presented, as well as methods for spectral assignment and for structure quality assessment. Second, the quantitative analysis of structure mobility i s reviewed.

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Untitled

Cited by 9 publications

References 4 publications

NMR Characterization of the Dynamics of Biomacromolecules

NMR Characterization of the Dynamics of Biomacromolecules

Characterization of the Fast Dynamics of Protein Amino Acid Side Chains Using NMR Relaxation in Solution

Quantitative Analysis of Biomolecular NMR Spectra: A Prerequisite for the Determination of the Structure and Dynamics of Biomolecules

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