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- W2035786823 endingPage "815" @default.
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- W2035786823 abstract "Activation of phospholipase A2 (PLA2) upon binding to phospholipid assemblies is poorly understood. X-ray crystallography revealed little structural change in the enzyme upon binding of monomeric substrate analogs, whereas small conformational changes in PLA2 complexed with substrate micelles and an inhibitor were found by NMR. The structure of PLA2 bound to phospholipid bilayers is not known. Here we uncover by FTIR spectroscopy a splitting in the alpha-helical region of the amide I absorbance band of PLA2 upon binding to lipid bilayers. We provide evidence that a higher frequency component, which is only observed in the membrane-bound enzyme, is a property of more flexible helices. Formation of flexible helices upon interaction with the membrane is likely to contribute to PLA2 activation." @default.
- W2035786823 created "2016-06-24" @default.
- W2035786823 creator A5021277644 @default.
- W2035786823 creator A5068810331 @default.
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- W2035786823 date "1997-05-01" @default.
- W2035786823 modified "2023-10-14" @default.
- W2035786823 title "Structural changes in a secretory phospholipase A2 Induced by membrane binding: a clue to interfacial activation?" @default.
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- W2035786823 doi "https://doi.org/10.1006/jmbi.1997.1014" @default.
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