Thermal Denaturation of Proteins and Chemical Equilibrium
نویسندگان
چکیده
منابع مشابه
Thermal Denaturation Equilibria of Tmv Coat Proteins
Thermal denaturation of RNA free coat proteins of tobacco mosaic virus (TMV) was studied for wildtype TMV (vulgare) and the temperature-sensitive mutant, Ni 118. The ability to form soluble aggregates as well as the optical properties (ORD, UV-difference spectra), and the sedimen tation behavior were used as criteria for the native state. At pH 7.5 , 7 = 0 .0 2 denaturation is reversible for b...
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The conformational stabilities of eight proteins in terms of the free energy differences between the native "folded" state of the protein and its "unfolded" state were determined at 298 K by two methods: chemical denaturation at 298 K and extrapolation to 298 K of the thermal denaturation results at high temperature. The proteins were expressed in Escherichia coli from the Haemophilus influenza...
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Finite size effects on the cooperative thermal denaturation of proteins are considered. A dimensionless measure of cooperativity, Omegac, scales as Nzeta, where N is the number of amino acids. Surprisingly, we find that zeta is universal with zeta=1+gamma, where the exponent gamma characterizes the divergence of the susceptibility for a self-avoiding walk. Our lattice model simulations and expe...
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Plasmas have a broad field of applications, such as air-breathing hypersonic vehicles (plasma control for scramjet engine), spacecraft atmospheric entries (influence of precursor electrons and prediction of blackout phenomenon), high-enthalpy wind tunnels (plasmatron, arc-jet, and shock tube facilities), lightning phenomena, discharges at atmospheric pressure, laboratory nuclear fusion and astr...
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The γS1- and γS2-crystallins, structural eye lens proteins from the Antarctic toothfish (Dissostichus mawsoni), are homologues of the human lens protein γS-crystallin. Although γS1 has the higher thermal stability of the two, it is more susceptible to chemical denaturation by urea. The lower thermodynamic stability of both toothfish crystallins relative to human γS-crystallin is consistent with...
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ژورنال
عنوان ژورنال: World Journal of Chemical Education
سال: 2015
ISSN: 2375-1665
DOI: 10.12691/wjce-3-3-1