Anharmonicity and self-similarity of the free energy landscape of protein G

dc.creator	Pontiggia, F.
dc.creator	Colombo, G.
dc.creator	Micheletti, C.
dc.creator	Orland, H.
dc.date	2006-12-12
dc.date.accessioned	2026-06-02T21:48:11Z
dc.description	The near-native free energy landscape of protein G is investigated through 0.4 microseconds-long atomistic molecular dynamics simulations in explicit solvent. A theoretical and computational framework is used to assess the time-dependence of salient thermodynamical features. While the quasi-harmonic character of the free energy is found to degrade in a few ns, the slow modes display a very mild dependence on the trajectory duration. This property originates from a striking self-similarity of the free energy landscape embodied by the consistency of the principal directions of the local minima, where the system dwells for several ns, and of the virtual jumps connecting them.
dc.description	revtex, 6 pages, 5 figures
dc.identifier	https://arxiv.org/abs/q-bio/0612020
dc.identifier	http://arxiv.org/abs/q-bio/0612020
dc.identifier	doi:10.1103/PhysRevLett.98.048102
dc.identifier.uri	https://demo.dspace.org/handle/10673/2625
dc.subject	Biomolecules
dc.subject	Soft Condensed Matter
dc.subject	Biological Physics
dc.title	Anharmonicity and self-similarity of the free energy landscape of protein G
dc.type	text

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