Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 46, Issue 2, Pages 250-254Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2009.12.013
Keywords
Aggregation; Alkaline unfolding; Circular dichroism
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Little work has been done to understand the folding of proteins at alkaline conditions. BSA acquires a partially reversible unfolded state at pH 13 0, devoid of any native structure Introduction of methanol, ethanol and 2-propanol with the alkaline unfolded protein resulted in beta-sheet-like structure formation, and 2,2,2-trifluroethanol found to enhance a-helical conformations with simultaneous increase in aggregation The extent of secondary and tertiary structure formation is in the order of methanol < ethanol < 2-propanol < 2,2.2-trifluroethanol Exposure of hydrophobic core of protein molecules in apolar environment of 2,2.2-trifluroethanol seems to promote intermolecular cluster formation This is one of the very few reports that a-helical structures can also aggregate (C) 2010 Elsevier B V All rights reserved
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