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- W2126031884 abstract "The CII protein of bacteriophage λ, which activates the synthesis of the λ repressor, plays a key role in the lysis–lysogeny switch. CII has a small in vivo half‐life due to its proteolytic susceptibility, and this instability is a key component for its regulatory role. The structural basis of this instability is not known. While studying guanidine hydrochloride‐assisted unfolding of CII, we found that low concentrations of the chaotrope (50–500 m m ) have a considerable effect on the structure of this protein. This effect is manifest in an increase in molar ellipticity, an enhancement of intrinsic tryptophan fluorescence intensity and a reduction in ANS binding. At low concentrations of guanidine hydrochloride CII is stabilized, as reflected in a significant decrease in the rate of proteolysis by trypsin and resistance to thermal aggregation, while the tetrameric nature of the protein is retained. Thus low concentrations of guanidine hydrochloride promote a more structured conformation of the CII protein. On the basis of these observations, a model has been proposed for the structure of CII wherein the protein equilibrates between a compact form and a proteolytically accessible form, in which the C‐terminal region assumes different structures." @default.
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- W2126031884 date "2003-10-19" @default.
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- W2126031884 title "Disorder-order transition of lambda CII promoted by low concentrations of guanidine hydrochloride suggests a stable core and a flexible C-terminus" @default.
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- W2126031884 doi "https://doi.org/10.1046/j.1432-1033.2003.03835.x" @default.
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