A Polymer Surfactant Corona Dynamically Replaces Water in Solvent-Free Protein Liquids and Ensures Macromolecular Flexibility and Activity

被引:44
作者
Gallat, Francois-Xavier [2 ,3 ,4 ,5 ]
Brogan, Alex P. S. [1 ]
Fichou, Yann [2 ,3 ,4 ]
McGrath, Nina [1 ]
Moulin, Martine [5 ,6 ]
Haertlein, Michael [5 ,6 ]
Combet, Jerome [5 ]
Wuttke, Joachim [7 ]
Mann, Stephen [1 ]
Zaccai, Giuseppe [2 ,3 ,4 ,5 ]
Jackson, Colin J. [8 ]
Perriman, Adam W. [1 ]
Weik, Martin [2 ,3 ,4 ,9 ]
机构
[1] Univ Bristol, Sch Chem, Ctr Organized Matter Chem, Bristol BS8 1TS, Avon, England
[2] Comissariat Energie Atom, Inst Biol Struct, F-38054 Grenoble, France
[3] CNRS, UMR5075, F-38027 Grenoble, France
[4] Univ Grenoble 1, F-38000 Grenoble, France
[5] Inst Max Von Laue Paul Langevin, F-38042 Grenoble 9, France
[6] Partnership Struct Biol, ILL EMBL Deuterat Lab, F-38042 Grenoble 9, France
[7] Forschungszentrum Julich, JCNS FRM 2, D-85747 Garching, Germany
[8] Australian Natl Univ, Res Sch Chem, Canberra, ACT 0200, Australia
[9] ESRF, F-38043 Grenoble, France
基金
英国工程与自然科学研究理事会; 欧盟第七框架计划;
关键词
NEUTRON-SCATTERING; HYDRATION WATER; LIGAND-BINDING; MYOGLOBIN; MOTIONS; SIMULATIONS; ENZYMES;
D O I
10.1021/ja303894g
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The observation of biological activity in solvent-free protein-polymer surfactant hybrids challenges the view of aqueous and nonaqueous solvents being unique promoters of protein dynamics linked to function. Here, we combine elastic incoherent neutron scattering and specific deuterium labeling to separately study protein and polymer motions in solvent-free hybrids. Myoglobin motions within the hybrid are found to closely resemble those of a hydrated protein, and motions of the polymer surfactant coating are similar to those of the hydration water, leading to the conclusion that the polymer surfactant coating plasticizes protein structures in a way similar to hydration water.
引用
收藏
页码:13168 / 13171
页数:4
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