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

Timothy M Ryan; Yun Xun; Nathan P Cowieson; Jitendra P Mata; Andrew Jackson; Brian R Pauw; Andrew J Smith; Nigel Kirby; Duncan McGillivray

doi:10.1016/j.bbrc.2016.03.135

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

Biochem Biophys Res Commun. 2016 May 13;473(4):834-839. doi: 10.1016/j.bbrc.2016.03.135. Epub 2016 Mar 29.

Authors

Timothy M Ryan¹, Yun Xun², Nathan P Cowieson³, Jitendra P Mata⁴, Andrew Jackson⁵, Brian R Pauw⁶, Andrew J Smith³, Nigel Kirby⁷, Duncan McGillivray⁸

Affiliations

¹ 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.
² 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.
³ Diamond Light Source Ltd., Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire, UK.
⁴ Bragg Institute, Australian Nuclear Science and Technology Organisation, New Illawarra Road, Lucas Heights, New South Wales, Australia.
⁵ European Spallation Source, Lund, Sweden.
⁶ Bundesanstalt für Materialforschung und -prüfung, Berlin, Germany.
⁷ Australian Synchrotron, Clayton, Victoria, Australia.
⁸ School of Chemical Science, The University of Auckland, Auckland, New Zealand; The MacDiarmid Institute of Advanced Materials and Nanotechnology, Wellington, New Zealand.

PMID: 27037018
DOI: 10.1016/j.bbrc.2016.03.135

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.

Keywords: High pressure; Protein unfolding; Ribonuclease A; SANS; SAXS; Small angle scattering.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Enzyme Activation
Enzyme Stability
Pressure*
Protein Conformation
Protein Denaturation*
Ribonuclease, Pancreatic / metabolism*
Ribonuclease, Pancreatic / ultrastructure
Structure-Activity Relationship
Temperature*

Substances

Ribonuclease, Pancreatic