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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
Author(s) -
Shalongo William,
Jagannadham Medicherla,
Stellwagen Earle
Publication year - 1993
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360330113
Subject(s) - chemistry , kinetic energy , guanidine , size exclusion chromatography , kinetics , globular protein , chromatography , folding (dsp implementation) , ribonuclease , thermodynamics , crystallography , organic chemistry , enzyme , rna , biochemistry , physics , quantum mechanics , electrical engineering , gene , engineering
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 partitioning and the conformational transition are described in terms of a finite difference algorithm incorporating an apparent binding model to generate broad and asymmetric peaks. Application of these equations to the simple two‐state unfolding transition of ribonuclease A in guanidine hydrochloride indicates that reliable kinetic parameters can be obtained using these equations. © 1993 John Wiley & Sons, Inc.