Abstract:
:The effect on the structure of profilin of phosphatidylinositol 4,5-bisphosphate (PIP2) binding was probed by fluorescence and circular dichroism (CD) spectroscopy. Fluorescence of Trp3 and Trp31 of profilin at 292 nm showed a linear decrease in solution emission at 340 nm as PIP2/profilin was increased from 0 to 80:1, apparently due to a static quenching mechanism involving formation of a nonfluorescent PIP2/profilin complex. CD spectra revealed an increase of up to 3.3-fold in the molar ellpticity at 222 nm for profilin as it binds PIP2, as well as changes in the Cotton effect between 250 and 310 nm. These results are consistent with a possible increase in the alpha-helix content of profilin triggered by the binding of PIP2.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Raghunathan V,Mowery P,Rozycki M,Lindberg U,Schutt Cdoi
10.1016/0014-5793(92)80324-akeywords:
subject
Has Abstractpub_date
1992-02-03 00:00:00pages
46-50issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(92)80324-Ajournal_volume
297pub_type
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