Combined pressure and temperature denaturation of ribonuclease A produces alternate denatured states

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dc.contributor.authorRyan, TMen_AU
dc.contributor.authorXun, Yen_AU
dc.contributor.authorCowieson, NPen_AU
dc.contributor.authorMata, JPen_AU
dc.contributor.authorJackson, AJen_AU
dc.contributor.authorPauw, BRen_AU
dc.contributor.authorSmith, AJen_AU
dc.contributor.authorKirby, Nen_AU
dc.contributor.authorMcGillivray, DJen_AU
dc.date.accessioned2023-11-17T03:11:01Zen_AU
dc.date.available2023-11-17T03:11:01Zen_AU
dc.date.issued2016-05-13en_AU
dc.date.statistics2023-11-16en_AU
dc.description.abstractProtein folding, unfolding and misfolding have become critically important to a range of health and industry applications. Increasing high temperature and high pressure are used to control and speed up reactions. A number of studies have indicated that these parameters can have a large effect on protein structure and function. Here we describe the additive effects of these parameters on the small angle scattering behaviour of ribonuclease A. We find that alternate unfolded structures can be obtained with combined high pressure and temperature treatment of the protein. © 2016 Elsevier Inc.en_AU
dc.description.sponsorshipThis research (SAXS) was undertaken on the SAXS/WAXS beamline at the Australian Synchrotron Victoria, Australia. This work was also carried out with the support of the Diamond Light Source. We acknowledge the support of the Bragg Institute, Australian Nuclear Science and Technology Organisation, in providing the neutron research facilities used in this work. T.R. is jointly funded by the Australian Synchrotron, The University of Auckland, The MacDiarmid Institute of Advanced Materials and Nanotechnology and The University of Canterbury.en_AU
dc.identifier.citationRyan, T. M., Xun, Y., Cowieson, N. P., Mata, J. P., Jackson, A., Pauw, B. R., Smith, A. J., Kirby, N., & McGillivray, D. (2016). Combined pressure and temperature denaturation of ribonuclease A produces alternate denatured states. Biochemical and Biophysical Research Communications, 473(4), 834-839. doi:10.1016/j.bbrc.2016.03.135en_AU
dc.identifier.issn0006-291Xen_AU
dc.identifier.issue4en_AU
dc.identifier.journaltitleBiochemical and Biophysical Research Communicationsen_AU
dc.identifier.pagination834-839en_AU
dc.identifier.urihttps://apo.ansto.gov.au/handle/10238/15204en_AU
dc.identifier.volume473en_AU
dc.language.isoenen_AU
dc.publisherElsevieren_AU
dc.relation.urihttps://doi.org/10.1016/j.bbrc.2016.03.135en_AU
dc.subjectProtein denaturationen_AU
dc.subjectRNA-ASEen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectNeutron diffractionen_AU
dc.subjectProteinsen_AU
dc.subjectProtein structureen_AU
dc.titleCombined pressure and temperature denaturation of ribonuclease A produces alternate denatured statesen_AU
dc.typeJournal Articleen_AU
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