Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1979546 | Current Opinion in Structural Biology | 2008 | 6 Pages |
Abstract
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 μs 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?
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Authors
R Dustin Schaeffer, Alan Fersht, Valerie Daggett,