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Structural changes in profilin accompany its binding to phosphatidylinositol 4,5‐bisphosphate
Author(s) -
Raghunathan Vidya,
Mowery Patrick,
Rozycki Michael,
Lindberg Uno,
Schutt Clarence
Publication year - 1992
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 - 10.1016/0014-5793(92)80324-a
Subject(s) - profilin , chemistry , phosphatidylinositol , circular dichroism , quenching (fluorescence) , fluorescence , biophysics , helix (gastropod) , fluorescence spectroscopy , binding site , biochemistry , stereochemistry , biology , phosphorylation , ecology , actin cytoskeleton , physics , cytoskeleton , snail , cell , quantum mechanics
The effect on the structure of profilin of phosphatidylinositol 4,5‐bisphosphate (PIP 2 ) binding was probed by fluorescence and circular dichroism (CD) spectroscopy, Fluorescence of Trp 3 and Trp 31 of profilin at 292 nm showed a linear decrease in solution emission at 340 nm as PIP 2 /profilin was increased from 0 to 80:1, apparently due to a static quenching mechanism involving formation of a nonfluorescent PIP 2 /profilin complex. CD spectra revealed an increase of up to 3.3‐fold in the molar ellipticity at 222 nm for profilin as it binds PIP 2 , as well as changes in the Cotton effect between 250 and 310 nm. These results are consistent with a possible increase in the α‐helix content or profilin triggered by the binding or PIP 2 .