This title appears in the Scientific Report :
2012
Please use the identifier:
http://dx.doi.org/10.1021/ja303894g in citations.
A Polymer Surfactant Corona Dynamically Replaces Water in Solvent-Free Protein Liquids and Ensures Macromolecular Flexibility and Activity
A Polymer Surfactant Corona Dynamically Replaces Water in Solvent-Free Protein Liquids and Ensures Macromolecular Flexibility and Activity
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 se...
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Personal Name(s): | Gallat, F.-X. |
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Brogan, A.P.S. / Fichou, Y. / McGrath, N. / Moulin, M. / Härtlein, M. / Combet, J. / Wuttke, J. / Mann, S. / Zaccai, G. / Jackson, C.J. / Perriman, A.W. / Weik, M. | |
Contributing Institute: |
Neutronenstreuung; ICS-1 Neutronenstreuung; JCNS-1 JCNS-FRM-II; JCNS-FRM-II |
Published in: | Journal of the American Chemical Society, 134 (2012) S. 13168 |
Imprint: |
Washington, DC
American Chemical Society
2012
|
Physical Description: |
13168 |
PubMed ID: |
22853639 |
DOI: |
10.1021/ja303894g |
Document Type: |
Journal Article |
Research Program: |
Integrated Infrastructure Initiative for Neutron Scattering and Muon Spectroscopy In-house Research with PNI BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |
Series Title: |
Journal of the American Chemical Society
134 |
Subject (ZB): | |
Publikationsportal JuSER |
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. |