Thermodynamics of Protein Denaturation.
نویسندگان
چکیده
منابع مشابه
Protein Denaturation on p-T Axes--Thermodynamics and Analysis.
Proteins are essential players in the vast majority of molecular level life processes. Since their structure is in most cases substantial for their correct function, study of their structural changes attracted great interest in the past decades. The three dimensional structure of proteins is influenced by several factors including temperature, pH, presence of chaotropic and cosmotropic agents, ...
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 کاملRole of solvation effects in protein denaturation: from thermodynamics to single molecules and back.
Protein stability often is studied in vitro through the use of urea and guanidinium chloride, chemical cosolvents that disrupt protein native structure. Much controversy still surrounds the underlying mechanism by which these molecules denature proteins. Here we review current thinking on various aspects of chemical denaturation. We begin by discussing classic models of protein folding and how ...
متن کاملPressure and protein denaturation.
Kinetic analyses have indicated that moderate hydrostatic pressures, up to some 700 atmospheres, oppose reversible and irreversible denaturations of certain enzyme systems, apparent at temperatures above the normal optimum of the enzyme reaction, as well as at lower temperatures in the presence of denaturants such as alcohol (14). Qualitative observations have shown that such pressures also ret...
متن کاملLigand-induced biphasic protein denaturation.
The results of a thermodynamic calculation of the excess heat capacity that is based on experimental observations and that incorporates the effects of ligand binding on the two-state, thermal denaturation of a protein are presented. For a protein with a single-binding site on the native species and at subsaturating concentrations of ligand, bimodal or unimodal thermograms were computed merely b...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 1995
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.35.3