Unfolding of Bovine Heart Cytochrome c Induced by Urea and Guanidine Hydrochloride

Bian, Liujiao; Tan, Zhijian; Yang, Xinlin; Liu, Li; Zheng, Xiaohao

doi:10.1002/cjoc.201190163

Cited by 3 publications

(2 citation statements)

References 32 publications

(23 reference statements)

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“…As shown in our previous work, the unfolding of the bovine heart cytochrome c induced by both guanidine hydrochloride and urea is a typical two-state process [34]. Besides, in our previous work, the structure changes of bovine heart cytochrome c during the two unfolding processes were also studied.…”

Section: Resultsmentioning

confidence: 82%

“…In previous work, we determined the intrinsic fluorescence emission spectrum, fluorescence phase diagram, and fluorescence quenching and deactivation profile for the unfolding of bovine heart cytochrome c induced by urea and guanidine hydrochloride and found that the unfolding of bovine heart cytochrome c induced by both guanidine hydrochloride and urea was a typical two-state process [34] .…”

Section: Methodsmentioning

confidence: 99%

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Distribution, Transition and Thermodynamic Stability of Protein Conformations in the Denaturant-Induced Unfolding of Proteins

Bian

2014

PLoS ONE

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BackgroundExtensive and intensive studies on the unfolding of proteins require appropriate theoretical model and parameter to clearly illustrate the feature and characteristic of the unfolding system. Over the past several decades, four approaches have been proposed to describe the interaction between proteins and denaturants, but some ambiguity and deviations usually occur in the explanation of the experimental data.Methodology/Principal FindingsIn this work, a theoretical model was presented to show the dependency of the residual activity ratio of the proteins on the molar denaturant concentration. Through the characteristic unfolding parameters k i and Δm i in this model, the distribution, transition and thermodynamic stability of protein conformations during the unfolding process can be quantitatively described. This model was tested with the two-state unfolding of bovine heart cytochrome c and the three-state unfolding of hen egg white lysozyme induced by both guanidine hydrochloride and urea, the four-state unfolding of bovine carbonic anhydrase b induced by guanidine hydrochloride and the unfolding of some other proteins induced by denaturants. The results illustrated that this model could be used accurately to reveal the distribution and transition of protein conformations in the presence of different concentrations of denaturants and to evaluate the unfolding tendency and thermodynamic stability of different conformations. In most denaturant-induced unfolding of proteins, the unfolding became increasingly hard in next transition step and the proteins became more unstable as they attained next successive stable conformation.Conclusions/SignificanceThis work presents a useful method for people to study the unfolding of proteins and may be used to describe the unfolding and refolding of other biopolymers induced by denaturants, inducers, etc.

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Section: Resultsmentioning

confidence: 82%

Section: Methodsmentioning

confidence: 99%