A graph theoretical analysis of the energy landscape of model proteins

The study of the dynamics of systems characterized by a rough energy
landscape, such as strctural glasses and protein models, is
often amenable to a master equation approach.
Depending on temperature different groups of energy minima define
different metastable states which are interconnected via a web of
transition states thus defining a temperature dependent 'connectivity
graph'.
The topology of such graphs is investigated in different protein models
showing a correlation between their spectral dimension and the
frustration and folding propensity of the peptide analyzed.
This analysis serioulsy challenges the description of the folding
process in terms of reaction coordinates holding spectral dimension
values that sistematically exceed unity.