caa a22 4500 445327723 CHVBK 20180317142726.0 cr unu---uuuuu 170323e20110901xx s 000 0 eng 10.1007/s10953-011-9737-8 doi (NATIONALLICENCE)springer-10.1007/s10953-011-9737-8 Thermodynamic Studies of Amino Acid-Denaturant Interactions in Aqueous Solutions at 298.15 K [Elektronische Daten] [Deepti Kurhe, Dilip Dagade, Jyoti Jadhav, Sanjay Govindwar, Kesharsingh Patil] As proteins and other biomolecules consisting of amino acid residues require external additives for their dissolution and recrystallization, it is important to have information about how such additives interact with amino acids. Therefore we have studied the interactions of simple model amino acids with the additives urea and guanidine hydrochloride in aqueous solutions at 298.15K, using vapor pressure osmometry. During the measurements, the concentration of urea was fixed as ∼2 mol⋅kg−1 and that of guanidine hydrochloride was fixed as ∼1 mol⋅kg−1 whereas the concentrations of amino acids were varied. The experimental water activity data were processed to get the individual activity coefficients of all the three components in the ternary mixture. Further, the activity coefficients were used to get the excess Gibbs energies of solutions and Gibbs energies for transfer of either amino acids from water to aqueous denaturant solutions or denaturant from water to aqueous amino acid solutions. An application of the McMillan-Mayer theory of solutions through virial expansion of transfer Gibbs energies was made to get pair and triplet interaction parameter whose sign and magnitude yielded information about amino acid-denaturant interactions, relative to their interactions with water. The pair interaction parameters have been further used to obtain salting constants and in turn the thermodynamic equilibrium constant values for the amino acid-denaturant mixing process in aqueous solutions at 298.15K. The results have been explained in terms of hydrophobic hydration, hydrophobic interactions and amino acid-denaturant binding. Springer Science+Business Media, LLC, 2011 Amino acids nationallicence Protein denaturant nationallicence Osmometry nationallicence Hydrophobic hydration nationallicence Hydrophobic effect nationallicence Thermodynamic equilibrium constant nationallicence Kurhe Deepti Department of Biochemistry, Shivaji University, 416004, Kolhapur, India aut Dagade Dilip Department of Chemistry, Shivaji University, 416004, Kolhapur, India aut Jadhav Jyoti Department of Biochemistry, Shivaji University, 416004, Kolhapur, India aut Govindwar Sanjay Department of Biochemistry, Shivaji University, 416004, Kolhapur, India aut Patil Kesharsingh School of Chemical Sciences, North Maharashtra University, Jalgaon, India aut Journal of Solution Chemistry Springer US; http://www.springer-ny.com 40/9(2011-09-01), 1596-1617 0095-9782 40:9<1596 2011 40 10953 https://doi.org/10.1007/s10953-011-9737-8 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10953-011-9737-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kurhe Deepti Department of Biochemistry, Shivaji University, 416004, Kolhapur, India aut NATIONALLICENCE 700 1- Dagade Dilip Department of Chemistry, Shivaji University, 416004, Kolhapur, India aut NATIONALLICENCE 700 1- Jadhav Jyoti Department of Biochemistry, Shivaji University, 416004, Kolhapur, India aut NATIONALLICENCE 700 1- Govindwar Sanjay Department of Biochemistry, Shivaji University, 416004, Kolhapur, India aut NATIONALLICENCE 700 1- Patil Kesharsingh School of Chemical Sciences, North Maharashtra University, Jalgaon, India aut NATIONALLICENCE 773 0- Journal of Solution Chemistry Springer US; http://www.springer-ny.com 40/9(2011-09-01), 1596-1617 0095-9782 40:9<1596 2011 40 10953 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer