Experimental studies of protein folding reactions often have complex kinetic and thermodynamic properties that reflect the presence of partially-folded states that appear along folding pathways. Relating the relatively sparse data obtained from spectroscopic methods, e.g., CD, FL and SAXS, to the structures of the folding intermediates remains a major challenges in understanding the readout from 1D sequence information to 3D structure. In several successful collaborations with the Brooks group, we have come to appreciate the power of coarse-grained simulations of folding reactions in interpreting experimental data and providing testable predictions of the structures of transient intermediates. Experimental and computational studies of CheY, a 129 aa ba-repeat protein, and SsIGPS, a 222 aa TIM barrel protein, illustrate the advantages of the combined approach.<br/>This work was supported by the National Science Foundation and the National Institutes of Health.

Simulation and experiment: The power of a combined approach to protein folding and dynamics

251st National Meeting (2016)

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