Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme.

Journal article

Quenched-flow hydrogen exchange labeling, monitored by 1H NMR and electrospray ionization mass spectrometry (ESI-MS), has been employed in conjunction with stopped-flow circular dichroism and fluorescence to study the kinetic refolding from guanidinium chloride of a derivative of hen lysozyme in which one of the four disulfide linkages (Cys6-Cys127) has been selectively chemically reduced and carboxymethylated (CM6,127-lysozyme). Removal of this disulfide bridge has little effect on the struc...

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Authors: Eyles, S; Radford, SE; Robinson, C; Dobson, C

• Publication status: Published
• Journal: Biochemistry
• Volume: 33
• Issue: 44
• Pages: 13038-13048
• Publication date: 1994-11-01
• DOI: 10.1021/bi00248a013
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Chickens; Kinetics; Biological Transport; Animals; Disulfides; Spectrometry, Fluorescence; Protein Conformation; Reference Standards; Female; Magnetic Resonance Spectroscopy; Cysteine; Mass Spectrometry; Protein Folding; Hydrogen; Muramidase; Circular Dichroism