Éditeur(s) : HAL CCSD Elsevier
Résumé : International audience
The discerning behavior of living systems relies on accurate interactions selected from the lot of molecular collisions occurring in the cell. To ensure the reliability of interactions, binding partners are classically envisioned as finely preadapted molecules, selected on the basis of their affinity in one-step associations. But the counterselection of inappropriate interactions can in fact be much more efficiently obtained through difficult multi-step adjustment, whose final high energy state is locked by a fluctuation ratchet. The progressive addition of molecular bonds during stereo-adjustment can be modeled as a predominantly backward random walk whose first arrival is frozen by a micro-irreversible transition. A new criterion of ligand specificity is presented, that is based on the ratio rejection/incorporation. In addition to its role in the selectivity of interactions, this generic recipe can underlie other important biological phenomena such as the regular synthesis at low level of supramolecular complexes, monostable kinetic bimodality, substrate concentration thresholds or the preparation of rapidly depolymerizable structures with stored energy, like microtubules
ISSN: 0079-6107

hal-01274234
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01274234
DOI : 10.1016/j.pbiomolbio.2016.02.001
PUBMED : 26867859

Éditeur(s) : HAL CCSD Royal Society of Chemistry
Résumé : International audience
A full equilibrium treatment of molecular aggregation is presented for prototypes of 1D and 3D aggregates, with and without nucleation. By skipping complex kinetic parameters like aggregate size-dependent diffusion, the equilibrium treatment allows to predict directly time-independent quantities such as critical concentrations. The relationships between the macroscopic equilibrium constants for the different paths are first established by statistical corrections and so as to comply with the detailed balance constraints imposed by nucleation, and the composition of the mixture resulting from homogeneous aggregation is then analyzed using the polylogarithm function. Several critical concentrations are distinguished: the residual monomer concentation in equilibrium (RMC) and the critical nucleation concentration (CNC), that is the threshold concentration of total subunits necessary for initiating aggregation. When increasing the concentration of total subunits, the RMC converges more strongly to its asymptotic value, the equilibrium constant of depolymerization, for 3D aggregates and in case of nucleation. The CNC moderately depends on the number of subunits in the nucleus, but sharply increases with the difference between the equilibrium constants of polymerization and nucleation. As the RMC and CNC can be numerically but not analytically determined, ansatz equations connecting them to thermodynamic parameters are proposed
PCCP : Physical chemistry chemical physics

Droits : info:eu-repo/semantics/OpenAccess
hal-01565995
https://hal.archives-ouvertes.fr/hal-01565995
https://hal.archives-ouvertes.fr/hal-01565995/document
https://hal.archives-ouvertes.fr/hal-01565995/file/Aggregates_in_equilibrium.pdf
DOI : 10.1039/c6cp08369b

Éditeur(s) : HAL CCSD Springer Verlag (Germany)
Résumé : International audience
The Michaelis-Menten enzymatic reaction is sufficient to perceive many subtleties of network modeling, including the concentration and time scales separations, the formal equivalence between bulk phase and single-molecule approaches, or the relationships between single-cycle transient probabilities and steady state rates. Twelve methods proposed by different authors and yielding the same famous Michaelis-Menten equation, are selected here to illustrate the kinetic and probabilistic use of rate constants and to review basic techniques for handling them. Finally, the general rate of an ordered multistep reaction, of which the Michaelis-Menten reaction is a particular case, is deduced from a Markovian approach.
ISSN: 0259-9791

hal-00920806
https://hal-univ-rennes1.archives-ouvertes.fr/hal-00920806
https://hal-univ-rennes1.archives-ouvertes.fr/hal-00920806v2/document
https://hal-univ-rennes1.archives-ouvertes.fr/hal-00920806/file/12MM.pdf
ARXIV : 1312.5468

Éditeur(s) : HAL CCSD Springer Verlag (Germany)
Résumé : International audience
The Michaelis-Menten enzymatic reaction is sufficient to perceive many subtleties of network modeling, including the concentration and time scales separations, the formal equivalence between bulk phase and single-molecule approaches, or the relationships between single-cycle transient probabilities and steady state rates. Seven methods proposed by different authors and yielding the same famous Michaelis-Menten equation, are selected here to illustrate the kinetic and probabilistic use of rate constants and to review basic techniques for handling them. Finally, the general rate of an ordered multistep reaction, of which the Michaelis-Menten reaction is a particular case, is deduced from a Markovian approach.
Journal of Mathematical Chemistry

hal-00920806
https://hal-univ-rennes1.archives-ouvertes.fr/hal-00920806
https://hal-univ-rennes1.archives-ouvertes.fr/hal-00920806/document
ARXIV : 1312.5468
DOI : 10.1007/s10910-013-0237-5