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Review
. 2008 Feb;18(1):4-9.
doi: 10.1016/j.sbi.2007.11.007. Epub 2008 Feb 1.

Combining experiment and simulation in protein folding: closing the gap for small model systems

R Dustin Schaeffer  1 , Alan Fersht, Valerie Daggett
Affiliations
Review

Combining experiment and simulation in protein folding: closing the gap for small model systems

R Dustin Schaeffer et al. Curr Opin Struct Biol. 2008 Feb.

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 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?

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Figures

Figure 1
Figure 1
Chymotrypsin inhibitor 2 unfolds through its transition state to the denatured state, and then returns to a N′ state through the same transition state at 348K. This is the first observed case of microscopic reversibility in a simulation system.
See this image and copyright information in PMC

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