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Model Polymers Reveal New Clues to Protein Folding

nts a set of related pathways from the unfolded to the native state.

When Rokhsar and Pande repeated their simulations with model polymers of 64 and 80 mers, the folding pathways also grouped themselves into separate classes of intermediate states.

These intermediate phases are closely analogous to partially unfolded states (PUFs) which have been observed in real proteins, as well as to intermediate states inferred to exist in other real proteins. It is likely that knowledge of PUFs, plus inferences about similar phases from other protein studies, can predict transition states of some kinds of proteins in the real world. Rokhsar's and Pande's discovery of well-defined transition states in model-polymer folding has important implications for the development of a general theory of protein folding. Verifying these results using models with atomistic detail is the next important step.

IMAGES AVAILABLE ONLINE
The lattice model of protein folding can be seen in spectacular action by visiting http://hubbell.berkeley.edu/nsb.html. Also see
http://hubbell.berkeley.edu/graphics.html http://hubbell.berkeley.edu/home.html


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Contact: Paul Preuss
paul_preuss@lbl.gov
(510) 486-6249
DOE/Lawrence Berkeley National Laboratory
16-Feb-1999


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