In his famous 1959 review, Walter Kauzmann clarified important features of the thermodynamic stabilities of proteins. The hydrophobic effect is recognised as an important contributor to the stability of proteins and an important determinant of their structural patterns. As generally understood, it depends on the unusual properties of cold water and its interactions with nonpolar solutes. Here we comment on the relationship between this paradigm and the stabilities and structures of proteins from thermophilic organisms
The hydrophobic effect stabilizes the native structure of proteins by minimizing the unfavorable int...
Recent breakthroughs in the theory of hydrophobic effects permit new analyses of several characteris...
The hydrophobic effect appears to be a key driving force for many chemical and biological processes,...
The hydrophobic effect is considered the main driving force for protein folding and plays an importa...
Changes in free energy are normally used to track the effect of temperature on the stability of prot...
This chapter addresses question such as “If the hydrophobic theory of protein stability is correct, ...
We present a systematic computational investigation of the internal hydration of a set of homologous...
AbstractIn this paper, following our work on the two-state outer neighbor mixed bonding model of wat...
Three homologous proteins with mesophilic, thermophilic and hyperthermophilic character have been st...
AbstractExperimental evidence suggests that proteins adsorbed to hydrophobic surfaces at low coverag...
P(論文)Protein has a hydrophobic surface within its molecule, therefor the protein molecule dissolved ...
The Lum–Chandler–Weeks theory of hydrophobicity [Lum, K., Chandler, D. & Weeks, J. D. (1999) J. Phys...
The hydrophobic effect is a major driving force in protein folding. A complete understanding of this...
In this work, we address the question of whether the enhanced stability of thermophilic proteins has...
It is known that protein misfolding is governed by the hydrophobic effect of solutes at hydrophobic ...
The hydrophobic effect stabilizes the native structure of proteins by minimizing the unfavorable int...
Recent breakthroughs in the theory of hydrophobic effects permit new analyses of several characteris...
The hydrophobic effect appears to be a key driving force for many chemical and biological processes,...
The hydrophobic effect is considered the main driving force for protein folding and plays an importa...
Changes in free energy are normally used to track the effect of temperature on the stability of prot...
This chapter addresses question such as “If the hydrophobic theory of protein stability is correct, ...
We present a systematic computational investigation of the internal hydration of a set of homologous...
AbstractIn this paper, following our work on the two-state outer neighbor mixed bonding model of wat...
Three homologous proteins with mesophilic, thermophilic and hyperthermophilic character have been st...
AbstractExperimental evidence suggests that proteins adsorbed to hydrophobic surfaces at low coverag...
P(論文)Protein has a hydrophobic surface within its molecule, therefor the protein molecule dissolved ...
The Lum–Chandler–Weeks theory of hydrophobicity [Lum, K., Chandler, D. & Weeks, J. D. (1999) J. Phys...
The hydrophobic effect is a major driving force in protein folding. A complete understanding of this...
In this work, we address the question of whether the enhanced stability of thermophilic proteins has...
It is known that protein misfolding is governed by the hydrophobic effect of solutes at hydrophobic ...
The hydrophobic effect stabilizes the native structure of proteins by minimizing the unfavorable int...
Recent breakthroughs in the theory of hydrophobic effects permit new analyses of several characteris...
The hydrophobic effect appears to be a key driving force for many chemical and biological processes,...