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...
Main Authors: | van den Berg, B, Chung, E, Robinson, C, Dobson, C |
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פורמט: | Journal article |
שפה: | English |
יצא לאור: |
1999
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פריטים דומים
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The origin of the alpha-domain intermediate in the folding of hen lysozyme.
מאת: Matagne, A, et al.
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The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase.
מאת: van den Berg, B, et al.
יצא לאור: (1999) -
Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme.
מאת: Eyles, S, et al.
יצא לאור: (1994) -
NMR studies of the dynamics and the folding of hen lysozyme
מאת: Buck, M, et al.
יצא לאור: (1994)