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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Simplicity within the complexity: Bilateral impact of DMSO on the functional and unfolding patterns of α-chymotrypsin
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Simplicity within the complexity: Bilateral impact of DMSO on the functional and unfolding patterns of α-chymotrypsin

机译：复杂性内的简单性：DMSO对α-胰凝乳蛋白酶功能和展开模式的双边影响

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摘要

New understanding of the fundamental links between protein stability, conformational flexibility and function, can be gained through synergic studies on their catalytic and folding/unfolding properties under the influence of stabilizing/destabilizing additives. We explored an impact of dimethyl sulfoxide (DMSO), the moderate effector of multilateral action, on the kinetic (functional) and thermodynamic (thermal unfolding) patterns of a hydrolytic enzyme, α-chymotrypsin (a-CT), over a wide range of additive concentrations, 0-70% (v/v). Both the calorimetric and kinetic data exhibited rich behavior pointing to the complex interplay of global/local stability (and flexibility) patterns. The complex action of DMSO is explained through the negative and positive preferential solvation motifs that prevail for the extreme opposite, native-like and unfolded states, respectively, implying essential stabilization of compact domains by enhancement of interfacial water networks and destabilization of a flexible active site by direct binding of DMSO to the unoccupied specific positions intended for elongated polypeptide substrates.
机译：通过在稳定/去稳定添加剂的影响下对它们的催化和折叠/展开特性进行协同研究，可以获得对蛋白质稳定性，构象柔性和功能之间基本联系的新认识。我们探索了多边作用的中度效应物二甲基亚砜（DMSO）在广泛范围内对水解酶α-胰凝乳蛋白酶（a-CT）的动力学（功能）和热力学（热解折叠）模式的影响。添加剂浓度为0-70％（v / v）。量热和动力学数据均显示出丰富的行为，表明全局/局部稳定性（和灵活性）模式之间存在复杂的相互作用。 DMSO的复杂作用是通过分别在极端相反，天然样和未折叠状态下普遍存在的负和正优先溶剂化基序来解释的，这意味着通过增强界面水网络和破坏柔性活性位点来稳定紧凑域的本质通过直接将DMSO结合到打算用于拉长的多肽底物的未占据的特定位置上。

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