Exploring the Protein G Helix Free Energy Surface by Solute Tempering Metadynamics

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dc.creatorCamilloni, C.
dc.creatorProvasi, D.
dc.creatorTiana, G.
dc.creatorBroglia, R. A.
dc.date2007-07-09
dc.date.accessioned2026-07-07T08:14:38Z
dc.date.available2026-07-07T08:14:38Z
dc.descriptionThe free-energy landscape of the alpha-helix of protein G is studied by means of metadynamics coupled with a solute tempering algorithm. Metadynamics allows to overcome large energy barriers, whereas solute tempering improves the sampling with an affordable computational effort. From the sampled free-energy surface we are able to reproduce a number of experimental observations, such as the fact that the lowest minimum corresponds to a globular conformation displaying some degree of beta-structure, that the helical state is metastable and involves only 65% of the chain. The calculations also show that the system populates consistently a pi-helix state and that the hydrophobic staple motif is present only in the free-energy minimum associated with the helices, and contributes to their stabilization. The use of metadynamics coupled with solute tempering results then particularly suitable to provide the thermodynamics of a short peptide, and its computational efficiency is promising to deal with larger proteins.
dc.identifierhttps://arxiv.org/abs/0707.1230
dc.identifierhttp://arxiv.org/abs/0707.1230
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/133195
dc.subjectBiomolecules
dc.titleExploring the Protein G Helix Free Energy Surface by Solute Tempering Metadynamics
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