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

DOI: 10.1016/j.bbrc.2016.03.135 DOI Help

Authors: Timothy M. Ryan (Australian Synchrotron) , Yun Xun (Australian Synchrotron) , Nathan P. Cowieson (Diamond Light Source) , Jitendra P. Mata (Bragg Institute, Australian Nuclear Science and Technology Organisation) , Andrew Jackson (European Spallation Source) , Brian R. Pauw (Bundesanstalt für Materialforschung und -prüfung) , Andrew Smith (Diamond Light Source) , Nigel Kirby (Australian Synchrotron) , Duncan Mcgillivray (The University of Auckland)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochemical And Biophysical Research Communications

State: Published (Approved)
Published: March 2016

Abstract: Protein 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 ffect on protein structure and function. Here we describe the additive effects of these parameters on the small angle scattering behavior of ribonuclease A. We find that alternate unfolded structures can be obtained with combined high pressure and temperature treatment of the protein.

Journal Keywords: Protein unfolding; Small angle Scattering; SAXS; SANS; High pressure; Ribonuclease A

Subject Areas: Chemistry


Instruments: I22-Small angle scattering & Diffraction

Other Facilities: Australian Synchrotron and ANSTO (Australian neutron source)