The assembly mechanism for aggregation of amyloid fibril is important and fundamental for any quantitative and physical descriptions because it needs to have a deep understanding of both molecular and statistical physics. A theoretical model with three states including coil, helix and sheet is presented to describe the amyloid formation. The corresponding general mathematical expression of N molecule systems are derived, including the partition function and thermodynamic quantities. We study the equilibrium properties of the system in the solution and find that three molecules have the extreme value of free energy. The denaturant effect on molecular assemble is also discussed. Furthermore, we apply the kinetic theories to take account of th...
We propose an exactly solvable simplified statistical mechanical model for the thermodynamics of bet...
International audienceProtein polymerization consists in the aggregation of single monomers into pol...
International audienceMore than twenty types of proteins can adopt misfolded conformations, which ca...
The assembly mechanism for aggregation of amyloid fibril is important and fundamental for any quanti...
AbstractWe develop a theory for three states of equilibrium of amyloid peptides: the monomer, oligom...
Amyloidlike proteins form highly organized aggregates, such as fibrils and plaques, preceded by the ...
Amyloidlike proteins form highly organized aggregates, such as fibrils and plaques, preceded by the ...
Protein misfolding and concomitant aggregation towards amyloid formation is the underlying biochemic...
Intermolecular noncovalent interactions between protein molecules result in the formation of a wide ...
A simple lattice-gas model, with two fundamental energy terms —elongation and nucleation effects, is...
Starting from a disordered aggregate, we have simulated the formation of ordered amyloid-like beta s...
We present and study a minimal structure-based model for the self-assembly of peptides into ordered ...
The classical nucleation theory finds the rate of nucleation proportional to the monomer concentrati...
More than twenty types of proteins can adopt misfolded conforma-tions, which can co-aggregate into a...
Despite the complexity and the specificity of the amino acid code, a variety of peptides and protein...
We propose an exactly solvable simplified statistical mechanical model for the thermodynamics of bet...
International audienceProtein polymerization consists in the aggregation of single monomers into pol...
International audienceMore than twenty types of proteins can adopt misfolded conformations, which ca...
The assembly mechanism for aggregation of amyloid fibril is important and fundamental for any quanti...
AbstractWe develop a theory for three states of equilibrium of amyloid peptides: the monomer, oligom...
Amyloidlike proteins form highly organized aggregates, such as fibrils and plaques, preceded by the ...
Amyloidlike proteins form highly organized aggregates, such as fibrils and plaques, preceded by the ...
Protein misfolding and concomitant aggregation towards amyloid formation is the underlying biochemic...
Intermolecular noncovalent interactions between protein molecules result in the formation of a wide ...
A simple lattice-gas model, with two fundamental energy terms —elongation and nucleation effects, is...
Starting from a disordered aggregate, we have simulated the formation of ordered amyloid-like beta s...
We present and study a minimal structure-based model for the self-assembly of peptides into ordered ...
The classical nucleation theory finds the rate of nucleation proportional to the monomer concentrati...
More than twenty types of proteins can adopt misfolded conforma-tions, which can co-aggregate into a...
Despite the complexity and the specificity of the amino acid code, a variety of peptides and protein...
We propose an exactly solvable simplified statistical mechanical model for the thermodynamics of bet...
International audienceProtein polymerization consists in the aggregation of single monomers into pol...
International audienceMore than twenty types of proteins can adopt misfolded conformations, which ca...