A jump model has been used to obtain motional information from proton relaxation parameters in complex molecular systems in which multiple internal motions are present. The proposed analysis takes into account changes in orientation and magnitude of interproton vectors, due to overall and internal motions. Intrinsic relaxation contributions can be calculated if the probability for each spatial configuration is independently known. From these contributions jump frequencies may be evaluated, yielding information on local molecular mobility. © 1982 Società Italiana di Fisica
matrix, ROESY, spectral density functions Comparatively small molecules such as peptides can show a ...
[[abstract]]Interproton NMR dipolar cross-relaxation rates have been calculated from a 1-ns molecula...
Longitudinal and transverse proton relaxation rates have been measured for L-histidine in water solu...
A jump model has been used to obtain motional information from proton relaxation parameters in compl...
The internal motions of biomolecules were examined by analyzing NMR relaxation in terms of the model...
International audienceDuring the past decades, NMR spectroscopy has emerged as a unique tool for the...
The method proposed in the companion paper for analysing the coupling between overall and internal d...
Models based on the neglect of the coupling of the overall molecular rotations with the conformation...
The model compound N-acetyl-L-phenylalanine methyl ester was used to investigate the motional behavi...
Since many biological processes occur on the μs to ms time scale, internal dynamics on that time sca...
In order to study the effect of internal dynamics on the accuracy of NMR structures in detail, we ge...
A formalism based on the theory of Markov processes and suitable for the analysis of multiple intern...
A general framework is presented for the interpretation of NMR relaxation data of proteins. The meth...
The description of the reorientational dynamics of flexible molecules is a challenging task, in part...
Internal motions in proteins, such as oscillations of internuclear vectors u(NiHiN) of amide bonds a...
matrix, ROESY, spectral density functions Comparatively small molecules such as peptides can show a ...
[[abstract]]Interproton NMR dipolar cross-relaxation rates have been calculated from a 1-ns molecula...
Longitudinal and transverse proton relaxation rates have been measured for L-histidine in water solu...
A jump model has been used to obtain motional information from proton relaxation parameters in compl...
The internal motions of biomolecules were examined by analyzing NMR relaxation in terms of the model...
International audienceDuring the past decades, NMR spectroscopy has emerged as a unique tool for the...
The method proposed in the companion paper for analysing the coupling between overall and internal d...
Models based on the neglect of the coupling of the overall molecular rotations with the conformation...
The model compound N-acetyl-L-phenylalanine methyl ester was used to investigate the motional behavi...
Since many biological processes occur on the μs to ms time scale, internal dynamics on that time sca...
In order to study the effect of internal dynamics on the accuracy of NMR structures in detail, we ge...
A formalism based on the theory of Markov processes and suitable for the analysis of multiple intern...
A general framework is presented for the interpretation of NMR relaxation data of proteins. The meth...
The description of the reorientational dynamics of flexible molecules is a challenging task, in part...
Internal motions in proteins, such as oscillations of internuclear vectors u(NiHiN) of amide bonds a...
matrix, ROESY, spectral density functions Comparatively small molecules such as peptides can show a ...
[[abstract]]Interproton NMR dipolar cross-relaxation rates have been calculated from a 1-ns molecula...
Longitudinal and transverse proton relaxation rates have been measured for L-histidine in water solu...