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- W2012172012 abstract "Equilibrium guanidinium chloride (GdmCI)-induced unfolding of arginine kinase (AK) was investigated by enzymatic activity, intrinsic fluorescence, 8-anilinonaphthalene-1-sulfonic acid (ANS) fluorescence, circular dichroism (CD) spectrum, and size-exclusion chromatography. The measurements showed that AK unfolded through two equilibrium intermediates: the molten globule state and the partly folded state. Both intermediates have no enzyme activity. The molten globule state exists at 0.4–0.8 mol/L GdmCI, perhaps after the N-terminal domain has unfolded but the C-terminal domain is still intact. The partly folded state occurs at 1.1–1.5 mol/L GdmCI with a hydrodynamic volume no more than 1.6-fold larger than the native state and a pronounced far UV-CD signal. Its ANS fluorescence intensity is about 50% of the molten globule state. This partly folded state shares similarities with the “burst” kinetic intermediate of protein folding." @default.
- W2012172012 created "2016-06-24" @default.
- W2012172012 creator A5026948419 @default.
- W2012172012 creator A5046860067 @default.
- W2012172012 creator A5062919352 @default.
- W2012172012 creator A5087057497 @default.
- W2012172012 date "2005-08-01" @default.
- W2012172012 modified "2023-09-26" @default.
- W2012172012 title "Characteristics of two intermediates trapped in the unfolding pathway of arginine kinase induced by guanidinium chloride" @default.
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- W2012172012 doi "https://doi.org/10.1016/s1007-0214(05)70101-2" @default.
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