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Simulations of a protein fold switch reveal crowding-induced population shifts driven by disordered regions - Communications Chemistry

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Simulations of a protein fold switch reveal crowding-induced population shifts driven by disordered regions - Communications Chemistry

Macromolecular crowding effects on globular proteins, which usually adopt a single stable fold, have been widely studied. However, little is known about crowding effects on fold-switching proteins, which reversibly switch between distinct folds. Here we study the mutationally driven switch between the folds of GA and GB, the two 56-amino acid binding domains of protein G, using a structure-based dual-basin model.

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Simulations of a protein fold switch reveal crowding-induced population shifts driven by disordered regions - Communications Chemistry

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Simulations of a protein fold switch reveal crowding-induced population shifts driven by disordered regions - Communications Chemistry

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