| Research at Medicine |
| Emeritus Professor Peter Barry |
 | Phone: 02 9385 1101 |  |
| Email: |
| Qualifications: BSc, PhD Syd, DSc UNSW |
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| School/Unit: |
| School of Medical Sciences
Department of Physiology |
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| Broad Research Areas: | |
| Neuroscience
Physiology | |
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| Specific Research Keywords: | |
| Ion Channels
Structure & Function of Ion Channels
Liquid Junction Potentials
Ligand gated ion channels
Unstirred Layer Effects | |
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| Research Interests: | |
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These include investigating the relationship between the molecular structure and the physiological function of channels such as those of the inhibitory neurotransmitter receptor glycine and the olfactory cyclic nucleotide-gated channel, investigating the factors that determine their ion selectivity and conductance, together with the mechanisms underlying olfactory transduction and the role different ionic channels in that phenomenon. Other interests include evaluating errors arising from liquid junction potentials in membrane potential measurements (with the development of a software program, JPCalc, to do that; see http://www.med.unsw.edu.au/PHBSoft) and the role of unstirred-layers in biological phenomena |
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| Teaching Interests: | |
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These include the teaching of membrane and cellular physiology and development of some interactive graphical computer-based teaching programs (ArtMem, MemPot and MemCable; see: http://www.med.unsw.edu.au/PHBSoft), which demonstrate some fairly difficult concepts in electrophysiology by simulating actual experiments, which relate to the electrical properties of cells and the development of membrane potentials across biological membrane. Other teaching software is related to illustrating the movements of ions, solutes and water across biological membranes and phenomena that result from unstirred layers adjacent to them |
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| Society Memberships & Professional Activities: | |
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President, Australian Society for Biophysics, 2003-2004;
Member, National Committee for Biomedical Sciences of the Australian Academy of Science, 2003-2005;
Emeritus member of The Biophysical Society (U.S.A.); Honorary member of The Australian Physiological and Pharmacological Society. Currently also a member of The Society of General Physiologists (U.S.A); The Australian Society for Biophysics; The Australian Neuroscience Society; Association for Chemoreception Sciences (AChemsS; USA).
Fellow of the Institute for the Study of Christianity in an Age of Science and Technology (ISCAST). |
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| Funding Sources: | |
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From 1986, virtually continuous support by NHMRC & ARC;
NHMRC Project (2003-2005): Barry, Moorhouse & Lewis "Structure-function studies of ion permeation and selectivity in recombinant glycine receptor channels"
ARC Discovery Project(2003-2005): Barry "A molecular structure function investigation of major membrane channels involved in olfactory transduction"
ARC Discovery Project(2005-2007): Moorhouse & Barry "Investigating the mechanisms of flavonoid actions in glycine receptors"
NHMRC Project (2007-2009): Schofield, Lewis, Barry & Clements "Mechanism of signal transduction and receptor activation in ligand gated ion channel receptors" |
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| Other Postgraduate Research: | |
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Potential thesis topics:
1. A molecular structure-physiological function investigation of the permeation and selectivity properties of the glycine neurotransmitter receptor channel
2. A molecular structure-physiological function investigation of the permeation and selectivity properties of the olfactory cyclic nucleotide-gated channel |
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| Key works/Publications: | |
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Barry, P.H., & Diamond, J.M. (1984). "Effects of unstirred layers on membrane phenomena." Physiol. Rev., 64: 763-872.
Barry, P.H. and Lynch, J.W. (1991). "Topical Review. Liquid junction potentials and small cell effects in patch clamp analysis." J. Membrane Biol. 121: 101-117.
Keramidas, A., Moorhouse, A.J., Pierce, K., Schofield, P.R. and Barry, P.H. (2002). Cation-selective mutations in the M2 domain of the inhibitory glycine receptor channel reveal determinants of ion-charge selectivity. J. Gen. Physiol. 119: 393-410 & Moorhouse et al., 119: 411-425.
Keramidas, A., Moorhouse, A.J., Schofield, P.R. and Barry, P.H. (2004). Ligand gated ion channels: Mechanisms underlying ion selectivity. Invited review for: Prog. Biophys. Molec. Biol., 86(2): 161-204.
Barry, P.H. and Lynch, J.W. (2005). Ligand-gated channels. IEEE Trans. Nanobiosci. 4(1) March: 70-80.
Qu, W., Moorhouse, A. J., Chandra, M., Lewis, T. M., Pierce, K. D. and Barry, P. H. (2006). A single P-loop glutamate point mutation to either lysine or arginine switches the cation-anion selectivity of the CNGA2 channel. J. Gen. Physiol. 127: 375-389.
Barry, P.H., Qu, W. and Moorhouse, A.J. (2008). Biophysics of CNG ion channels. In: Sensing with Ion Channels, Ed. B. Martinac, Springer Series in Biophysics, Springer-Verlag, pp. 175-200.
Sugiharto, S., T. M. Lewis, A. J. Moorhouse, P. R. Schofield, and P. H. Barry. 2008. Anion-cation permeability correlates with hydrated counter-ion size in glycine receptor channels. Biophys. J. 95: 4698-4715.  |
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| Further Information: | |
| http://medicalsciences.med.unsw.edu.au/SOMSWeb.nsf/page/Membrane+Biophysics+Lab | |
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