pH-dependent Stability and Membrane Interaction of the Pore-forming Domain of Colicin A*
作者： A. Muga , J.M. Gonzalez-Manas , J.H. Lakey , F. Pattus , W.K. Surewicz
DOI: 10.1016/S0021-9258(18)53888-6
关键词:
摘要: Thermal stability of the pore-forming domain colicin A was studied by high sensitivity differential scanning calorimetry and circular dichroism spectroscopy. In pH range between 8 5, thermal denaturation protein in solution occurs at 66-69 degrees C is characterized calorimetric enthalpy approximately 90 kcal/M. At below there a rapid pH-dependent destabilization resulting lowering midpoint temperature decrease denaturation. Circular spectra near far ultraviolet show that thermotropic transition associated with collapse native tertiary structure domain, although large proportion helical secondary remains preserved. The present data indicate some similarity also acid-induced temperature-induced A. Association phospholipid vesicles dioleoylphosphatidylglycerol results total disappearance transition, even values as 7. Since lipid binding induces spectrum, these interaction membrane facilitates conformational change within to looser (denaturated-like) state. These findings are discussed relation recent model (van der Goot, F. G., Gonzalez-Manas, J. M., Lakey, H., Pattus, (1991) Nature 354, 408-410) which postulates flexible "molten globule" state an intermediate on pathway insertion
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