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...
Κύριοι συγγραφείς: | van den Berg, B, Chung, E, Robinson, C, Dobson, C |
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Μορφή: | Journal article |
Γλώσσα: | English |
Έκδοση: |
1999
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Παρόμοια τεκμήρια
Παρόμοια τεκμήρια
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The origin of the alpha-domain intermediate in the folding of hen lysozyme.
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Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme.
ανά: Matagne, A, κ.ά.
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The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase.
ανά: van den Berg, B, κ.ά.
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Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme.
ανά: Eyles, S, κ.ά.
Έκδοση: (1994) -
NMR studies of the dynamics and the folding of hen lysozyme
ανά: Buck, M, κ.ά.
Έκδοση: (1994)