Báo cáo khoa học: The histidine-phosphocarrier protein of Streptomyces coelicolor folds by a partially folded species at low pH
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The folding of a 93-residue protein, the histidine-phospho-carrier protein ofStreptomyces coelicolor,HPr,hasbeenstudied using several biophysical techniques, namely fluo-rescence, 8-anilinonaphthalene-1-sulfate binding, circulardichroism, Fourier transform infrared spectroscopy, gelfiltration chromatography and differential scanning calori-metry. The chemical-denaturation behaviour of HPr, fol-lowed by fluorescence, CD and gel filtration, at pH 7.5 and25C, is described as a two-state process, which does notinvolve the accumulation of thermodynamically stableintermediates. Its conformational stability under those con-ditions isDG¼4.0 ± 0.2 kcalÆmol)1(1 kcal ¼4.18kJ),which makes the HPr fromS. coelicolorthe most unstablemember of the HPr family described so far. ...
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Báo cáo khoa học: The histidine-phosphocarrier protein of Streptomyces coelicolor folds by a partially folded species at low pH
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Báo cáo khoa học: The histidine-phosphocarrier protein of Streptomyces coelicolor folds by a partially folded species at low pH
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