Acid induced equilibrium unfolding of annexin V wild type shows two intermediate states.

Abstract:

:Annexin V is an alpha-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'.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Beermann ofm cap BB,Hinz HJ,Hofmann A,Huber R

doi

10.1016/s0014-5793(98)00105-7

subject

Has Abstract

pub_date

1998-02-20 00:00:00

pages

265-9

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014579398001057

journal_volume

423

pub_type

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