Characterisation of the dominant oxidative folding intermediate of hen lysozyme.
Reduced denatured lysozyme has been oxidised and refolded at pH values close to neutral in an efficient way by dilution from buffers containing 8.0 M urea, and refolding intermediates were separated by reverse-phase HPLC at pH 2. By using peptic digestion in combination with high-resolution Fourier...
المؤلفون الرئيسيون: | van den Berg, B, Chung, E, Robinson, C, Dobson, C |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
1999
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مواد مشابهة
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The origin of the alpha-domain intermediate in the folding of hen lysozyme.
حسب: Matagne, A, وآخرون
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Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme.
حسب: Matagne, A, وآخرون
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The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase.
حسب: van den Berg, B, وآخرون
منشور في: (1999) -
Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme.
حسب: Eyles, S, وآخرون
منشور في: (1994) -
NMR studies of the dynamics and the folding of hen lysozyme
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منشور في: (1994)