International audienceThe paper describes preliminary results of a molecular dynamics simulation study on the influence of non-denaturing hydrostatic pressure on the structure and the relaxation dynamics of lysozyme. The overall compression and the structural changes are in agreement with results from recent nuclear magnetic resonance experiments. We find that moderate hydrostatic pressure reduces essentially the amplitudes of the atomic motions, but does not change the characteristics of the slow internal dynamics. The latter is well described by a fractional Ornstein-Uhlenbeck process, concerning both single particle and collective motions
The cooperative nature of protein substructure and internal motion is a critical aspect of their fun...
High-pressure (15)N/(1)H NMR techniques were used to characterize the conformational fluctuations of...
We present here a study of the dynamics of two monomeric proteins, trypsin and lysozyme, by means of...
International audienceThe paper describes preliminary results of a molecular dynamics simulation stu...
International audienceThis paper presents a study of the influence of non-denaturing hydrostatic pre...
The motivation of the study presented here is to investigate how hydrostatic pressure influences the...
KNELLER G., Professeur, Université d'Orléans : Directeur de thèse BEE M., Professeur, Université Jos...
International audienceWe performed complementary inelastic neutron scattering (INS) experiments and ...
International audienceThe influence of high hydrostatic pressure on the internal sub-nanosecond dyna...
Constant pressure and temperature molecular dynamics techniques have been employed to investigate th...
AbstractIt is well known that proteins denature under high pressure. The mechanism that underlies su...
The “rules ” governing protein structure and stability are still poorly understood. Important clues ...
Small-angle X-ray scattering (SAXS) and elastic and quasi-elastic neutron scattering techniques were...
AbstractQuasielastic neutron and light-scattering techniques along with molecular dynamics simulatio...
Small-angle X-ray scattering (SAXS) and elastic and quasi-elastic neutron scattering techniques wer...
The cooperative nature of protein substructure and internal motion is a critical aspect of their fun...
High-pressure (15)N/(1)H NMR techniques were used to characterize the conformational fluctuations of...
We present here a study of the dynamics of two monomeric proteins, trypsin and lysozyme, by means of...
International audienceThe paper describes preliminary results of a molecular dynamics simulation stu...
International audienceThis paper presents a study of the influence of non-denaturing hydrostatic pre...
The motivation of the study presented here is to investigate how hydrostatic pressure influences the...
KNELLER G., Professeur, Université d'Orléans : Directeur de thèse BEE M., Professeur, Université Jos...
International audienceWe performed complementary inelastic neutron scattering (INS) experiments and ...
International audienceThe influence of high hydrostatic pressure on the internal sub-nanosecond dyna...
Constant pressure and temperature molecular dynamics techniques have been employed to investigate th...
AbstractIt is well known that proteins denature under high pressure. The mechanism that underlies su...
The “rules ” governing protein structure and stability are still poorly understood. Important clues ...
Small-angle X-ray scattering (SAXS) and elastic and quasi-elastic neutron scattering techniques were...
AbstractQuasielastic neutron and light-scattering techniques along with molecular dynamics simulatio...
Small-angle X-ray scattering (SAXS) and elastic and quasi-elastic neutron scattering techniques wer...
The cooperative nature of protein substructure and internal motion is a critical aspect of their fun...
High-pressure (15)N/(1)H NMR techniques were used to characterize the conformational fluctuations of...
We present here a study of the dynamics of two monomeric proteins, trypsin and lysozyme, by means of...