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...
| Auteurs principaux: | , , , , , |
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| Format: | Journal article |
| Langue: | English |
| Publié: |
1998
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