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In this study, a deuterium exchange procedure has been employed to evaluate the thermal stability of globular proteins under conditions that replicate their interactive behavior in reversed-phase high performance chromatographic (RP-HPLC) systems. In particular, this investigation has permitted the conformational stability of two proteins, hen egg white lysozyme (HEWL) and horse heart myoglobin (HMYO) to be examined under different temperature and low-pH solvent regimes. The results confirm that this experimental approach provides an efficient strategy to explore fundamental conformational features of polypeptides or proteins in their folded and partial unfolded states under these interactive conditions. In particular, this analytical procedure permits insight to be readily gained into the processes that occur when polypeptides and globular proteins interact with lipophilic liquid/ solid interfaces in the presence of water-organic solvent mixtures at different temperatures.

Item Type:	Refereed Article
Research Division:	Chemical Sciences
Research Group:	Analytical chemistry
Research Field:	Separation science
Objective Division:	Expanding Knowledge
Objective Group:	Expanding knowledge
Objective Field:	Expanding knowledge in the chemical sciences
UTAS Author:	Quirino, JP (Associate Professor Lito Quirino)
ID Code:	54785
Year Published:	2002
Web of Science® Times Cited:	8
Deposited By:	Austn Centre for Research in Separation Science
Deposited On:	2009-02-27
Last Modified:	2012-11-19
Downloads:	546 View Download Statistics