<p>Interactions between the protein and denaturant molecules in the denaturant-induced unfolding of proteins.</p
AbstractIn order to investigate the effect of concentration in biological processes such as protein ...
Both urea and guanidinium chloride (GdmCl) are frequently used as protein denaturants. Given that pr...
<p>Thermodynamics and stability of protein unfolding of single-chain and split NpuInts.</p
Extensive and intensive studies on the unfolding of proteins require appropriate theoretical model a...
Protein unfolding occurs when the balance of forces between the protein\u27s interaction with itself...
Protein denaturation refers to its specific spatial conformation change according to thecertain phys...
<p>N<i><sub>D</sub></i>, I<i><sub>Di</sub></i> and U<i><sub>D</sub></i> denote the native state, int...
<p>The interacting residues forms hydrogen bond, hydrophobic, and cation- π interactions are listed....
AbstractA denaturant-mediated protein unfolding model, which is different from already existing ones...
Proteins perform their function in their native folded state. The native folded state of a protein ...
<p>Interactions between adenine, ribose, and triphosphate parts of ATP and allosteric proteins.</p
Protein interactions, which include interactions between proteins and other biomolecules, are essent...
Protein denaturation is a decomposition process which is followed by chemical physical and biologgic...
Knowledge of protein stability is of utmost importance in various fields of biotechnology. Protein s...
AbstractElucidation of the mechanism of formation of insoluble protein aggregates is essential to re...
AbstractIn order to investigate the effect of concentration in biological processes such as protein ...
Both urea and guanidinium chloride (GdmCl) are frequently used as protein denaturants. Given that pr...
<p>Thermodynamics and stability of protein unfolding of single-chain and split NpuInts.</p
Extensive and intensive studies on the unfolding of proteins require appropriate theoretical model a...
Protein unfolding occurs when the balance of forces between the protein\u27s interaction with itself...
Protein denaturation refers to its specific spatial conformation change according to thecertain phys...
<p>N<i><sub>D</sub></i>, I<i><sub>Di</sub></i> and U<i><sub>D</sub></i> denote the native state, int...
<p>The interacting residues forms hydrogen bond, hydrophobic, and cation- π interactions are listed....
AbstractA denaturant-mediated protein unfolding model, which is different from already existing ones...
Proteins perform their function in their native folded state. The native folded state of a protein ...
<p>Interactions between adenine, ribose, and triphosphate parts of ATP and allosteric proteins.</p
Protein interactions, which include interactions between proteins and other biomolecules, are essent...
Protein denaturation is a decomposition process which is followed by chemical physical and biologgic...
Knowledge of protein stability is of utmost importance in various fields of biotechnology. Protein s...
AbstractElucidation of the mechanism of formation of insoluble protein aggregates is essential to re...
AbstractIn order to investigate the effect of concentration in biological processes such as protein ...
Both urea and guanidinium chloride (GdmCl) are frequently used as protein denaturants. Given that pr...
<p>Thermodynamics and stability of protein unfolding of single-chain and split NpuInts.</p
DOI
Add to ORKG