Complex network analysis of free-energy landscapes

The kinetics of biomolecular isomerization processes, such as protein folding, is governed by a free-energy surface of high dimensionality and complexity. As an alternative to projections into one or two dimensions, the free-energy surface can be mapped into a weighted network where nodes and links are configurations and direct transitions among them, respectively. In this work, the free-energy basins and barriers of the alanine dipepticle are determined quantitatively using an algorithm to partition the network into clusters (i.e., states) according to the equilibrium transitions sampled by molecular dynamics. The network-based approach allows for the analysis of the thermodynamics and kinetics of bionnolecule isomerization without reliance on arbitrarily chosen order parameters. Moreover, it is shown on low-dimensional models, which can be treated analytically, as well as for the alanine dipepticle, that the broad-tailed weight distribution observed in their networks originates from freeenergy basins with mainly enthalpic character.


Published in:
Proceedings Of The National Academy Of Sciences Of The United States Of America, 104, 1817-1822
Year:
2007
Publisher:
National Academy of Sciences
ISSN:
0027-8424
Keywords:
Laboratories:




 Record created 2010-03-17, last modified 2018-03-17


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