作者: Nirbhik Acharya , Prajna Mishra , Santosh Kumar Jha
DOI: 10.1021/ACS.JPCLETT.5B02545
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摘要: The role of van der Waals (vdW) packing interactions compared to the hydrophobic effect in stabilizing functional structure proteins is poorly understood. Here we show, using fluorescence resonance energy transfer, dynamic quenching, red-edge excitation shift, and near- far-UV circular dichroism, that pH-induced structural perturbation a multidomain protein leads formation state which two out three domains have characteristics dry molten globules, is, are expanded native with disrupted but cores. We quantitatively estimate energetic contribution vdW show they play an important stability cooperativity its transition, addition effect. Our results also indicate during unfolding, side-chain unlocking solvation occur distinct steps not a...