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Kinetic analysis of the hydrodynamic transition accompanying protein folding using size exclusion chromatography. 1. Denaturant dependent baseline changes

✍ Scribed by William Shalongo; Paul Heid; Earle Stellwagen

Publisher: Wiley (John Wiley & Sons)
Year: 1993
Tongue: English
Weight: 644 KB
Volume: 33
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360330112

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✦ Synopsis

Size exclusion profiles of proteins with persistent conformations exhibit broad asymmetric peaks whose shape and elution times are dependent on denaturant concentration. The collective elution profiles were precisely simulated by an apparent binding model that treats the denaturant dependence in terms of an apparent matrix binding. The model requires three experimentally measurable parameters: the elution time for the unbound protein, an apparent association equilibrium constant for binding, and an apparent exchange time for binding. The denaturant dependence for each of these parameters is related to the accessible surface area of the protein.

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Kinetic analysis of the hydrodynamic transition accompanying protein folding using size exclusion chromatography. 2. Comparison of spectral and chromatographic kinetic analyses

✍ William Shalongo; Medicherla Jagannadham; Earle Stellwagen 📂 Article 📅 1993 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 943 KB

The kinetics of the hydrodynamic volume change associated with the unfolding and refolding of a globular protein can be observed using high performance size exclusion chromatography. Chromatographic profiles that evidence such dynamics can be simulated using equations in which chromatographic partit