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Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solution
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SYSNO ASEP 0330761 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solution Title Spojení struktury a dynamiky: nedenaturizující vliv vysokého tlaku na lysozym v roztoku Author(s) Ortore, M. G. (IT)
Spinozzi, F. (IT)
Mariani, P. (IT)
Paciaroni, A. (IT)
Barbosa, L. R. S. (IT)
Amenitsch, H. (AT)
Steinhart, Miloš (UMCH-V) RID
Ollivier, J. (FR)
Russo, D. (FR)Source Title Journal of the Royal Society Interface. - : Royal Society Publishing - ISSN 1742-5689
Roč. 6, Suppl. 5 (2009), s. 619-634Number of pages 16 s. Language eng - English Country GB - United Kingdom Keywords lysozyme ; structure ; dynamics Subject RIV CD - Macromolecular Chemistry R&D Projects GESON/06/E005 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z40500505 - UMCH-V (2005-2011) UT WOS 000269826500007 DOI 10.1098/rsif.2009.0163.focus Annotation Small-angle X-ray scattering (SAXS) and elastic and quasi-elastic neutron scattering techniques were used to investigate the high-pressure-induced changes on interactions, the low-resolution structure and the dynamics of lysozyme in solution. SAXS data, analysed using a global-fit procedure based on a new approach for hydrated protein form factor description, indicate that lysozyme completely maintains its globular structure up to 1500 bar. Significant modifications however occur in the protein-protein interaction potential at approximately 600-1000 bar. Workplace Institute of Macromolecular Chemistry Contact Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358 Year of Publishing 2010
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