The origin of the alpha-domain intermediate in the folding of hen lysozyme.
Stopped-flow fluorescence and circular dichroism spectroscopy have been used in conjunction with quenched-flow hydrogen exchange labelling, monitored by electrospray ionization mass spectrometry, to compare the refolding kinetics of hen egg-white lysozyme at 20 degrees C and 50 degrees C. At 50 degr...
Main Authors: | Matagne, A, Chung, E, Ball, L, Radford, SE, Robinson, C, Dobson, C |
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Format: | Journal article |
Language: | English |
Published: |
1998
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