title: Combined pressure and temperature denaturation of ribonuclease A produces alternate denatured states.
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 effecton 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.
authors.affiliation: Australian Synchrotron, Clayton, Victoria, Australia; The MacDiarmid Institute of Advanced Materials and Nanotechnology, Wellington, New Zealand; The Florey Institute of Neuroscience and Mental Health, Parkville, Victoria, Australia. Electronic address: tim.ryan@synchrotron.org.au.
authors.forename: Timothy M
authors.initials: TM
authors.lastname: Ryan
authors.affiliation: Australian Synchrotron, Clayton, Victoria, Australia; School of Chemical Science, The University of Auckland, Auckland, New Zealand; The MacDiarmid Institute of Advanced Materials and Nanotechnology, Wellington, New Zealand.
authors.forename: Yun
authors.initials: Y
authors.lastname: Xun
authors.affiliation: Diamond Light Source Ltd., Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire, UK.
authors.forename: Nathan P
authors.initials: NP
authors.lastname: Cowieson
authors.affiliation: Bragg Institute, Australian Nuclear Science and Technology Organisation, New Illawarra Road, Lucas Heights, New South Wales, Australia.
authors.forename: Jitendra P
authors.initials: JP
authors.lastname: Mata
authors.affiliation: European Spallation Source, Lund, Sweden.
authors.forename: Andrew
authors.initials: A
authors.lastname: Jackson
authors.affiliation: Bundesanstalt für Materialforschung und -prüfung, Berlin, Germany.
authors.forename: Brian R
authors.initials: BR
authors.lastname: Pauw
authors.affiliation: Diamond Light Source Ltd., Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire, UK.
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Smith
authors.affiliation: Australian Synchrotron, Clayton, Victoria, Australia.
authors.forename: Nigel
authors.initials: N
authors.lastname: Kirby
authors.affiliation: School of Chemical Science, The University of Auckland, Auckland, New Zealand; The MacDiarmid Institute of Advanced Materials and Nanotechnology, Wellington, New Zealand.
authors.forename: Duncan
authors.initials: D
authors.lastname: McGillivray
mesh_terms: D004789:Enzyme Activation; D004795:Enzyme Stability; D011312:Pressure; D011487:Protein Conformation; D011489:Protein Denaturation; D012259:Ribonuclease, Pancreatic / Q000378:metabolism* / Q000648:ultrastructure; D013329:Structure-Activity Relationship; D013696:Temperature
chemical_list: D012259:Ribonuclease, Pancreatic
keywords: High pressure; Protein unfolding; Ribonuclease A; SANS; SAXS; Small angle scattering