Professeur des Universités, Sorbonne Université
Directeur de l’UMR8640
ENS – Département de chimie
24 rue Lhomond, 75005 Paris
Email: rodolphe.vuilleumier@ens.psl.eu
Phone: +33 144323324
Office: E119
We propose below 8 sections. Every member of the department can choose which one he/she wants to use. You can also use new ones. We only ask everyone to keep the general aspect of the page (no change of font, color, size, etc). For the picture, it must be 250px wide.
Short bio
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Education and professional experience
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Significant publications
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Publications
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2006
|
Determination of dihedral Ψ angles in large proteins by combining NHN/CαHα dipole/dipole cross-correlation and chemical shifts Article de journal K Loth; D Abergel; P Pelupessy; M Delarue; P Lopes; J Ouazzani; N Duclert-Savatier; M Nilges; G Bodenhausen; V Stoven Proteins: Structure, Function and Genetics, 64 (4), p. 931–939, 2006. @article{Loth:2006,
title = {Determination of dihedral Ψ angles in large proteins by combining NHN/CαHα dipole/dipole cross-correlation and chemical shifts},
author = {K Loth and D Abergel and P Pelupessy and M Delarue and P Lopes and J Ouazzani and N Duclert-Savatier and M Nilges and G Bodenhausen and V Stoven},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-33748455090&doi=10.1002%2fprot.21063&partnerID=40&md5=c6a8c64f4558525854e7c49aecaa379c},
doi = {10.1002/prot.21063},
year = {2006},
date = {2006-01-01},
journal = {Proteins: Structure, Function and Genetics},
volume = {64},
number = {4},
pages = {931--939},
abstract = {We propose a strategy based on the combination of experimental NH N/CαHα dipole/dipole cross-correlated relaxation rates and chemical shift analysis for the determination of Ψ torsion angles in proteins. The method allows the determination of a dihedral angle that is not easily accessible by nuclear magnetic resonance (NMR). The measurement of dihedral angle restraints can be used for structure calculation, which is known to improve the quality of NMR structures. The method is of particular interest in the case of large proteins, for which spectral assignment of the nuclear Overhauser effect spectra, and therefore straightforward structural determination, is out of reach. One advantage of the method is that it is reasonably simple to implement, and could be used in association with other methods aiming at obtaining structural information on complex systems, such as residual dipolar coupling measurements. An illustrative example is analyzed in the case of the 30-kDa protein 6-phosphogluconolactonase. © 2006 Wiley-Liss, Inc.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
We propose a strategy based on the combination of experimental NH N/CαHα dipole/dipole cross-correlated relaxation rates and chemical shift analysis for the determination of Ψ torsion angles in proteins. The method allows the determination of a dihedral angle that is not easily accessible by nuclear magnetic resonance (NMR). The measurement of dihedral angle restraints can be used for structure calculation, which is known to improve the quality of NMR structures. The method is of particular interest in the case of large proteins, for which spectral assignment of the nuclear Overhauser effect spectra, and therefore straightforward structural determination, is out of reach. One advantage of the method is that it is reasonably simple to implement, and could be used in association with other methods aiming at obtaining structural information on complex systems, such as residual dipolar coupling measurements. An illustrative example is analyzed in the case of the 30-kDa protein 6-phosphogluconolactonase. © 2006 Wiley-Liss, Inc. |
2005
|
A Markov model for relaxation and exchange in NMR spectroscopy Article de journal D Abergel; A G Palmer III Journal of Physical Chemistry B, 109 (11), p. 4837–4844, 2005. @article{Abergel:2005,
title = {A Markov model for relaxation and exchange in NMR spectroscopy},
author = {D Abergel and A G Palmer III},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-15744403441&doi=10.1021%2fjp0458304&partnerID=40&md5=af897563ec09b4f913cfdb6a9e2a226b},
doi = {10.1021/jp0458304},
year = {2005},
date = {2005-01-01},
journal = {Journal of Physical Chemistry B},
volume = {109},
number = {11},
pages = {4837--4844},
abstract = {A two-state Markov noise process for lattice fluctuations and chemical exchange dynamics is used to derive a stochastic Liouville equation describing the evolution of the spin-density operator in nuclear magnetic resonance spectroscopy. Relaxation through lattice fluctuations and chemical exchange processes is incorporated into the theory at the same fundamental level, and the results are valid for all time scales provided that lattice fluctuations are much faster than chemical exchange kinetics. Time-scale separation emerges as an essential feature from the lowest-order perturbation expansion of the average resolvent in the Laplace domain. © 2005 American Chemical Society.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
A two-state Markov noise process for lattice fluctuations and chemical exchange dynamics is used to derive a stochastic Liouville equation describing the evolution of the spin-density operator in nuclear magnetic resonance spectroscopy. Relaxation through lattice fluctuations and chemical exchange processes is incorporated into the theory at the same fundamental level, and the results are valid for all time scales provided that lattice fluctuations are much faster than chemical exchange kinetics. Time-scale separation emerges as an essential feature from the lowest-order perturbation expansion of the average resolvent in the Laplace domain. © 2005 American Chemical Society. |
2004
|
Cross-correlated relaxation in NMR of macromolecules in the presence of fast and slow internal dynamics Article de journal L Vugmeyster; P Pelupessy; B E Vugmeister; D Abergel; G Bodenhausen Comptes Rendus Physique, 5 (3), p. 377–386, 2004. @article{Vugmeyster:2004,
title = {Cross-correlated relaxation in NMR of macromolecules in the presence of fast and slow internal dynamics},
author = {L Vugmeyster and P Pelupessy and B E Vugmeister and D Abergel and G Bodenhausen},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-2442500664&doi=10.1016%2fj.crhy.2004.02.004&partnerID=40&md5=058f478a0487336127f7cb06974b859f},
doi = {10.1016/j.crhy.2004.02.004},
year = {2004},
date = {2004-01-01},
journal = {Comptes Rendus Physique},
volume = {5},
number = {3},
pages = {377--386},
abstract = {In this paper we present an analysis of correlation and spectral density functions involved in autorelaxation and cross-correlated relaxation in the magnetic resonance of macromolecules. Internal dynamics of the macromolecule are described in terms of two distinct fluctuation processes with different, slow and fast, correlation times. The approach developed in this work takes into account the possible coupling between both fluctuating internal processes. © 2004 Acad\'{e}mie des sciences. Published by Elsevier SAS. All rights reserved.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
In this paper we present an analysis of correlation and spectral density functions involved in autorelaxation and cross-correlated relaxation in the magnetic resonance of macromolecules. Internal dynamics of the macromolecule are described in terms of two distinct fluctuation processes with different, slow and fast, correlation times. The approach developed in this work takes into account the possible coupling between both fluctuating internal processes. © 2004 Académie des sciences. Published by Elsevier SAS. All rights reserved. |
A simple model for NMR relaxation in the presence of internal motions with dynamical coupling Article de journal D Abergel; G Bodenhausen Journal of Chemical Physics, 121 (2), p. 761–768, 2004. @article{Abergel:2004,
title = {A simple model for NMR relaxation in the presence of internal motions with dynamical coupling},
author = {D Abergel and G Bodenhausen},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-3242683501&doi=10.1063%2f1.1756867&partnerID=40&md5=8b7c4df05c38074ec58b2db8fd9dc701},
doi = {10.1063/1.1756867},
year = {2004},
date = {2004-01-01},
journal = {Journal of Chemical Physics},
volume = {121},
number = {2},
pages = {761--768},
abstract = {A simple model for NMR relaxation was investigated in the presence of internal motions with dynamical coupling. In the model, an interaction vector u undergoes a rotational diffusion motion both in its own, intrinsic, diffusion potential and in a coupling potential through which it is dynamically linked to a neighboring vector v. A linearized Langevin approach allows the derivation of explicit expressions for the correlation functions and for the corresponding order parameters. It was observed that the lattice affects the relaxation times measured by NMR through the spectral density function J(ω).},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
A simple model for NMR relaxation was investigated in the presence of internal motions with dynamical coupling. In the model, an interaction vector u undergoes a rotational diffusion motion both in its own, intrinsic, diffusion potential and in a coupling potential through which it is dynamically linked to a neighboring vector v. A linearized Langevin approach allows the derivation of explicit expressions for the correlation functions and for the corresponding order parameters. It was observed that the lattice affects the relaxation times measured by NMR through the spectral density function J(ω). |
34 Entrées « ‹ 2 de 2
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