[Folding@home] Slow unfolded-state structuring in Acyl-CoA binding protein folding revealed by simulation and experiment
Posted: Thu Dec 09, 2021 4:57 pm
J Am Chem Soc. 2012 Aug 1;134(30):12565-77. doi: 10.1021/ja302528z. Epub 2012 Jul 19. ABSTRACT Protein folding is a fundamental process in biology, key to understanding many human diseases. Experimentally, proteins often appear to fold via simple two- or three-state mechanisms involving mainly native-state interactions, yet recent network models built from atomistic simulations of small proteins suggest the existence of many possible metastable states and folding pathways. We reconcile these two pictures in a combined experimental and simulation study of acyl-coenzyme A binding protein (ACBP), a two-state folder (folding time ~10 ms) exhibiting residual unfolded-state structure, and a putative early folding intermediate. Using single-molecule FRET in conjunction with side-chain mutagenesis, we first demonstrate...
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