Reference : Unraveling the stability of polypeptide helices: Critical role of van der Waals inter...
Scientific journals : Article
Physical, chemical, mathematical & earth Sciences : Physics
http://hdl.handle.net/10993/25401
Unraveling the stability of polypeptide helices: Critical role of van der Waals interactions
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Tkatchenko, Alexandre mailto [Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, D-14195 Berlin, Germany]
Rossi, M. [Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, D-14195 Berlin, Germany]
Blum, V. [Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, D-14195 Berlin, Germany]
Ireta, J. [Departamento de Química, Universidad Autónoma Metropolitana-Iztapalapa, A.P. 55-534, México D. F. 09340, Mexico]
Scheffler, M. [Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, D-14195 Berlin, Germany]
2011
Physical Review Letters
106
11
Yes (verified by ORBilu)
International
00319007
[en] Ab initio molecular dynamics simulation ; Condensed phasis ; Dispersion force ; Functional capabilities ; Gasphase ; Gold standards ; Helical structures ; Intramolecular interactions ; Physiological environment ; Polypeptide helices ; Quantum-chemical calculation ; Thermal stability ; Time-scales ; Unfolding process ; Van der waals ; Van Der Waals interactions ; Amino acids ; Calculations ; Density functional theory ; Indoor air pollution ; Molecular dynamics ; Polypeptides ; Quantum chemistry ; Thermodynamic stability ; Van der Waals forces
[en] Folding and unfolding processes are important for the functional capability of polypeptides and proteins. In contrast with a physiological environment (solvated or condensed phases), an in vacuo study provides well-defined "clean room" conditions to analyze the intramolecular interactions that largely control the structure, stability, and folding or unfolding dynamics. Here we show that a proper consideration of van der Waals (vdW) dispersion forces in density-functional theory (DFT) is essential, and a recently developed DFT+vdW approach enables long time-scale ab initio molecular dynamics simulations at an accuracy close to "gold standard" quantum-chemical calculations. The results show that the inclusion of vdW interactions qualitatively changes the conformational landscape of alanine polypeptides, and greatly enhances the thermal stability of helical structures, in agreement with gas-phase experiments. © 2011 American Physical Society.
http://hdl.handle.net/10993/25401
10.1103/PhysRevLett.106.118102

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