14 research outputs found
Optical NRZ 2 × 10 Gbit/s polarisation division multiplex transmission with endless polarisation control driven by correlation signals
84 fs PMD detection sensitivity in 2 × 40 Gbit/s RZ polarisation multiplex transmission experiment
Optical polarisation-mode dispersion compensation of 2.4 bit durations of differential group delay at 40 Gbit/s
Polarisation mode dispersion compensation for 6 ps, 40 Gbit/s pulses using distributed equaliser in LiNbO3
Identifying Conformational-Selection and Induced-Fit Aspects in the Binding-Induced Folding of PMI from Markov State Modeling of Atomistic Simulations
Unstructured
proteins and peptides typically fold during binding
to ligand proteins. A challenging problem is to identify the mechanism
and kinetics of these binding-induced folding processes in experiments
and atomistic simulations. In this Article, we present a detailed
picture for the folding of the inhibitor peptide PMI into a helix
during binding to the oncoprotein fragment <sup>25–109</sup>Mdm2 obtained from atomistic, explicit-water simulations and Markov
state modeling. We find that binding-induced folding of PMI is highly
parallel and can occur along a multitude of pathways. Some pathways
are induced-fit-like with binding occurring prior to PMI helix formation,
while other pathways are conformational-selection-like with binding
after helix formation. On the majority of pathways, however, binding
is intricately coupled to folding, without clear temporal ordering.
A central feature of these pathways is PMI motion on the Mdm2 surface,
along the binding groove of Mdm2 or over the rim of this groove. The
native binding groove of Mdm2 thus appears as an asymmetric funnel
for PMI binding. Overall, binding-induced folding of PMI does not
fit into the classical picture of induced fit or conformational selection
that implies a clear temporal ordering of binding and folding events.
We argue that this holds in general for binding-induced folding processes
because binding and folding events in these processes likely occur
on similar time scales and do exhibit the time-scale separation required
for temporal ordering
Journal officiel de la République française. Lois et décrets
05 avril 18861886/04/05 (A18,N94).Appartient à l’ensemble documentaire : MAEDIGen0Appartient à l’ensemble documentaire : MAEDI008Appartient à l’ensemble documentaire : MAEDI012Appartient à l’ensemble documentaire : MAEDI006Appartient à l’ensemble documentaire : MAEDI00
Identifying Conformational-Selection and Induced-Fit Aspects in the Binding-Induced Folding of PMI from Markov State Modeling of Atomistic Simulations
Unstructured
proteins and peptides typically fold during binding
to ligand proteins. A challenging problem is to identify the mechanism
and kinetics of these binding-induced folding processes in experiments
and atomistic simulations. In this Article, we present a detailed
picture for the folding of the inhibitor peptide PMI into a helix
during binding to the oncoprotein fragment <sup>25–109</sup>Mdm2 obtained from atomistic, explicit-water simulations and Markov
state modeling. We find that binding-induced folding of PMI is highly
parallel and can occur along a multitude of pathways. Some pathways
are induced-fit-like with binding occurring prior to PMI helix formation,
while other pathways are conformational-selection-like with binding
after helix formation. On the majority of pathways, however, binding
is intricately coupled to folding, without clear temporal ordering.
A central feature of these pathways is PMI motion on the Mdm2 surface,
along the binding groove of Mdm2 or over the rim of this groove. The
native binding groove of Mdm2 thus appears as an asymmetric funnel
for PMI binding. Overall, binding-induced folding of PMI does not
fit into the classical picture of induced fit or conformational selection
that implies a clear temporal ordering of binding and folding events.
We argue that this holds in general for binding-induced folding processes
because binding and folding events in these processes likely occur
on similar time scales and do exhibit the time-scale separation required
for temporal ordering
Identifying Conformational-Selection and Induced-Fit Aspects in the Binding-Induced Folding of PMI from Markov State Modeling of Atomistic Simulations
Unstructured
proteins and peptides typically fold during binding
to ligand proteins. A challenging problem is to identify the mechanism
and kinetics of these binding-induced folding processes in experiments
and atomistic simulations. In this Article, we present a detailed
picture for the folding of the inhibitor peptide PMI into a helix
during binding to the oncoprotein fragment <sup>25–109</sup>Mdm2 obtained from atomistic, explicit-water simulations and Markov
state modeling. We find that binding-induced folding of PMI is highly
parallel and can occur along a multitude of pathways. Some pathways
are induced-fit-like with binding occurring prior to PMI helix formation,
while other pathways are conformational-selection-like with binding
after helix formation. On the majority of pathways, however, binding
is intricately coupled to folding, without clear temporal ordering.
A central feature of these pathways is PMI motion on the Mdm2 surface,
along the binding groove of Mdm2 or over the rim of this groove. The
native binding groove of Mdm2 thus appears as an asymmetric funnel
for PMI binding. Overall, binding-induced folding of PMI does not
fit into the classical picture of induced fit or conformational selection
that implies a clear temporal ordering of binding and folding events.
We argue that this holds in general for binding-induced folding processes
because binding and folding events in these processes likely occur
on similar time scales and do exhibit the time-scale separation required
for temporal ordering
Identifying Conformational-Selection and Induced-Fit Aspects in the Binding-Induced Folding of PMI from Markov State Modeling of Atomistic Simulations
Unstructured
proteins and peptides typically fold during binding
to ligand proteins. A challenging problem is to identify the mechanism
and kinetics of these binding-induced folding processes in experiments
and atomistic simulations. In this Article, we present a detailed
picture for the folding of the inhibitor peptide PMI into a helix
during binding to the oncoprotein fragment <sup>25–109</sup>Mdm2 obtained from atomistic, explicit-water simulations and Markov
state modeling. We find that binding-induced folding of PMI is highly
parallel and can occur along a multitude of pathways. Some pathways
are induced-fit-like with binding occurring prior to PMI helix formation,
while other pathways are conformational-selection-like with binding
after helix formation. On the majority of pathways, however, binding
is intricately coupled to folding, without clear temporal ordering.
A central feature of these pathways is PMI motion on the Mdm2 surface,
along the binding groove of Mdm2 or over the rim of this groove. The
native binding groove of Mdm2 thus appears as an asymmetric funnel
for PMI binding. Overall, binding-induced folding of PMI does not
fit into the classical picture of induced fit or conformational selection
that implies a clear temporal ordering of binding and folding events.
We argue that this holds in general for binding-induced folding processes
because binding and folding events in these processes likely occur
on similar time scales and do exhibit the time-scale separation required
for temporal ordering