Abstract: The apparent specific volume, j2, of a-chymotrypsinogen A (a-ctg A) in a aqueous solutions containing different amount of urea, methylurea, N,N’-dimethylurea or ethylurea was determined from density measurements. Since no dependence of j2 on protein concentration was observed its values were equated with the corresponding specific volumes at the infinite dilution, v 20. The small positive changes in v 20 observed in urea and methylurea solutions at the highest denaturant concentration were ascribed to the complete unfolding of a-ctg A while significantly larger positive changes observed in N,N’-dimethylurea and ethylurea solutions were explained in terms of the incomplete unfolding of a-ctg A into a compact intermediate state
A comparison has been made among the values of the enthalpic pairwise interaction coefficients of tw...
The influences of various solute molecules upon the structure of water have been investigated by mea...
Chemistry Research Lab, Deshbandhu College, University of Delhi, New Delhi- 11 0 019, India E-mail ...
The partial specific volume of ~-lactoglobulin A in 0.02 M NaCl - 0.01 M HCl containing different am...
Urea has been known as a strong denaturant for globular proteins. Numerous papers have been publishe...
The interactions of a-chymotrypsinogen A with urea, methyl-, N,N\u27-dimethyl-, ethyl-, N,N\u27-diet...
We describe a statistical thermodynamic approach to analyzing urea-dependent volumetric properties o...
The focus of this research was to understand the role of bulk water in protein-folding equilibria. ...
AbstractThe critical urea concentration (C3∗) which destabilizes the structure of bovine serum album...
The work performed in this dissertation is devoted to understanding and quantifying solute-solvent i...
We report that the presence of very low concentrations (50.1M) of urea, a widely used chemical denat...
This thesis is devoted to understanding solute-solvent interactions in folded and unfolded proteins....
Urea is widely used as protein denaturant in aqueous solutions. Experiments and computer simulation ...
grantor: University of TorontoWe have used model proteins to study the role of water in tw...
<p>Solvent properties of aqueous media (dipolarity/polarizability, hydrogen bond donor acidity, and ...
A comparison has been made among the values of the enthalpic pairwise interaction coefficients of tw...
The influences of various solute molecules upon the structure of water have been investigated by mea...
Chemistry Research Lab, Deshbandhu College, University of Delhi, New Delhi- 11 0 019, India E-mail ...
The partial specific volume of ~-lactoglobulin A in 0.02 M NaCl - 0.01 M HCl containing different am...
Urea has been known as a strong denaturant for globular proteins. Numerous papers have been publishe...
The interactions of a-chymotrypsinogen A with urea, methyl-, N,N\u27-dimethyl-, ethyl-, N,N\u27-diet...
We describe a statistical thermodynamic approach to analyzing urea-dependent volumetric properties o...
The focus of this research was to understand the role of bulk water in protein-folding equilibria. ...
AbstractThe critical urea concentration (C3∗) which destabilizes the structure of bovine serum album...
The work performed in this dissertation is devoted to understanding and quantifying solute-solvent i...
We report that the presence of very low concentrations (50.1M) of urea, a widely used chemical denat...
This thesis is devoted to understanding solute-solvent interactions in folded and unfolded proteins....
Urea is widely used as protein denaturant in aqueous solutions. Experiments and computer simulation ...
grantor: University of TorontoWe have used model proteins to study the role of water in tw...
<p>Solvent properties of aqueous media (dipolarity/polarizability, hydrogen bond donor acidity, and ...
A comparison has been made among the values of the enthalpic pairwise interaction coefficients of tw...
The influences of various solute molecules upon the structure of water have been investigated by mea...
Chemistry Research Lab, Deshbandhu College, University of Delhi, New Delhi- 11 0 019, India E-mail ...