Combining experiment and simulation in protein folding: closing the gap for small model systems.
All-atom molecular dynamics (MD) simulations on increasingly powerful computers have been combined with experiments to characterize protein folding in detail over wider time ranges. The folding of small ultrafast folding proteins is being simulated on micros timescales, leading to improved structural predictions and folding rates. To what extent is 'closing the gap' between simulation and experiment for such systems providing insights into general mechanisms of protein folding?
Schaeffer
R Dustin
RD
Biomolecular Structure & Design Program, University of Washington, Seattle, WA 98195, USA.
Fersht
Alan
A
Daggett
Valerie
V
D000818:Animals; D003198:Computer Simulation; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D014508:Urea / Q000737:chemistry; D014867:Water / Q000737:chemistry
D011506:Proteins; D014867:Water; D014508:Urea