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The free-energy landscape of the alpha-helix of protein G is studied by meansof metadynamics coupled with a solute tempering algorithm. Metadynamics allowsto overcome large energy barriers, whereas solute tempering improves thesampling with an affordable computational effort. From the sampled free-energysurface we are able to reproduce a number of experimental observations, such asthe fact that the lowest minimum corresponds to a globular conformationdisplaying some degree of beta-structure, that the helical state is metastableand involves only 65% of the chain. The calculations also show that the systempopulates consistently a pi-helix state and that the hydrophobic staple motifis present only in the free-energy minimum associated with the helices, andcontributes to their stabilization. The use of metadynamics coupled with solutetempering results then particularly suitable to provide the thermodynamics of ashort peptide, and its computational efficiency is promising to deal withlarger proteins.

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