Competitive Model on Denaturant-Mediated Protein Unfolding
نویسندگان
چکیده
منابع مشابه
in silico evaluation of crosslinking effects on denaturant meq values and δcp upon protein unfolding
important thermodynamic parameters including denaturant equilibrium m values (meq) and heat capacity changes (δcp) can be predicted based on changes in solvent accessible surface area (sasa) upon unfolding. crosslinks such as disulfide bonds influence the stability of the proteins by decreasing the entropy gain as well as reduction of sasa of unfolded state. the aim of the study was to develop ...
متن کاملIn silico Evaluation of Crosslinking Effects on Denaturant m eq values and ΔCp upon Protein Unfolding
Important thermodynamic parameters including denaturant equilibrium m values (m(eq)) and heat capacity changes (ΔCp) can be predicted based on changes in Solvent Accessible Surface Area (SASA) upon unfolding. Crosslinks such as disulfide bonds influence the stability of the proteins by decreasing the entropy gain as well as reduction of SASA of unfolded state. The aim of the study was to develo...
متن کاملThermodynamics of denaturant-induced unfolding of a protein that exhibits variable two-state denaturation.
Free energy changes (DeltaG(degrees)(N-->D)) obtained by denaturant-induced unfolding using the linear extrapolation method (LEM) are presumed to reflect the stability differences between native (N) and denatured (D) species in the absence of denaturant. It has been shown that with urea and guanidine hydrochloride (GdnHCl) some proteins exhibit denaturant-independent (DeltaG(degrees)(N-->D)). B...
متن کاملDistribution, Transition and Thermodynamic Stability of Protein Conformations in the Denaturant-Induced Unfolding of Proteins
BACKGROUND Extensive 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 ...
متن کاملProtein Unfolding and the Diffusion Collision Model
In the diffusion-collision model, the unfolding or backward rates are given by the likelihood of secondary structural cluster dissociation. In this work, we introduce a backward rate calculation modeled from a Kramers-type thermal tunneling through a barrier, which represents the free energy potential well for buried hydrophobic residues. Our results are in good agreement with currently accepte...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2003
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(03)74896-6