Research Output for C. Austen Angell
Note: The 2012, 2013 publications have not been audited.
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C. Austen Angell may be from another institution or only recently joined Deakin University.
Publications
2010 External
Byrne, Nolene and Angell, C. Austen* (2010) The solubility of Hen lysozyme in ethylammonium nitrate / H20 mixtures : a novel approach to protein crystallization, Molecules journal, vol. 15, no. 2, pp. 793-803, M D P I AG, Basel, Switzerland [C1.1]
ERA journal ID: 22271 – Scopus EID: 2-s2.0-77649213682
Citation counts:Scopus - 8,
Thomson - 8
DRO entry for this publication
2009 External
Byrne, N* and Angell C. A.* (2009) Protein folding in the protic ionic liquid milieu : from native conformation to fibril, Chimica oggi : Chemistry today, vol. 27, no. 1, pp. 51-53, Teknoscienze, Milan, Italy [C1.1]
ERA journal ID: 40695 – Scopus EID: 2-s2.0-63849178829
Citation counts:Byrne, Nolene* and Angell, C. Austen* (2009) Formation and dissolution of hen egg white lysozyme amyloid fibrils in protic ionic liquids, Chemical communications, pp. 1046-1048, Royal Society of Chemistry, London, England [C1.1]
ERA journal ID: 1319 – Scopus EID: 2-s2.0-61849106912
Citation counts:Byrne, Nolene*, Belieres, Jean-Philippe* and Austen Angell, C.* (2009) The "refoldability" of selected proteins in ionic liquids as a stabilization criterion, leading to a conjecture on biogenesis, Australian journal of chemistry, vol. 62, no. 4, pp. 328-333, CSIRO Publishing, Collingwood, Vic [C1.1]
ERA journal ID: 1314 – Scopus EID: 2-s2.0-67649172877
Citation counts:Cho, Theresa Y.*, Byrne, Nolene*, Moore, David J.*, Pethica, Brian A.*, Angell, C. Austen* and Debenedetti, Pablo G.* (2009) Structure–energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state, Chemical communications, vol. 29, pp. 4441-4443, Royal Society of Chemistry, Cambridge, England [C1.1]
ERA journal ID: 1319 – Scopus EID: 2-s2.0-70249085617
Citation counts:Ping, Wen*, Harrowell, Peter*, Byrne, Nolene* and Angell, C. Austen* (2009) Composition dependence of the solid state transitions in NaNO3/KNO3 mixtures, Thermochimica acta, vol. 486, no. 1-2, pp. 27-31, Elsevier BV, Amsterdam, Netherlands [C1.1]
ERA journal ID: 1511 – Scopus EID: 2-s2.0-60349117242
Citation counts:2008 External
Byrne, N.* and Angell. C. A,* (2008) Protein unfolding, and the "tuning in" of reversible intermediate, states in protic ionic liquid media, Journal of molecular biology, vol. 378, no. 3, pp. 707-714, Academic Press, London, England [C1.1]
ERA journal ID: 2239 – Scopus EID: 2-s2.0-42249087622
Citation counts:2007 External
Angell, C. Austen*, Byrne. Nolene* and Belieres, Jean-Philippe* (2007) Parallel developments in aprotic and protic ionic liquids : physical chemistry and applications, Accounts of chemical research, vol. 40, no. 11, pp. 1228-1236, American Chemical Society, Washington, D. C. [C1.1]
ERA journal ID: 41361 – Scopus EID: 2-s2.0-37349076236
Citation counts:Byrne, Nolene*, Wang, Li-Min*, Belieres, Jean-Philippe* and Angell, C. Austen* (2007) Reversible folding–unfolding, aggregation protection, and multi-year stabilization, in high concentration protein solutions, using ionic liquids, Chemical communications, no. 26, pp. 2714-2716, Royal Society of Chemistry, Cambridge, England [C1.1]
ERA journal ID: 1319 – Scopus EID: 2-s2.0-34347229082
Citation counts:
Grants and Consultancies
No grants and/or consultancies found or audited – the 2012 HERDC financial return has not been completed or loaded as yet.
Higher Degree by Research Completions supervised by C. Austen Angell
No completions found or audited.
- Legend:
- * Not a member of Deakin University at time of output.
DRO to publications collection last synchronised: Wednesday 22nd May 2013 10:04pm
