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Acid induced equilibrium unfolding of annexin V wild type shows two intermediate states
Author(s) -
Beermann Br.Bernd,
Hinz Hans-Jürgen,
Hofmann Andreas,
Huber Robert
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00105-7
Subject(s) - circular dichroism , chemistry , exocytosis , annexin , molten globule , crystallography , biophysics , biochemistry , membrane , biology , cell
Annexin V is an α‐helical protein which shows anticoagulatory and antiinflammatory activity. It is supposed to be involved in membrane fusion and exocytosis. In this study acid‐induced equilibrium unfolding of the human annexin V is investigated by fluorescence and circular dichroism spectroscopy. The spectroscopic data indicate that at least two intermediate states are involved in unfolding. One of the proposed intermediate states exhibits properties similar to those observed with annexin V wild type saturated with calcium, another may be regarded as ‘molten globule’.