Amino acid/water interactions study: a new amino acid scale |
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| Authors: | Pedro P Madeira Ana Bessa Luís Álvares-Ribeiro M Raquel Aires-Barros Alírio E Rodrigues Vladimir N Uversky |
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| Institution: | 1. Laboratory of Separation and Reaction Engineering, Departamento de Engenharia Química, Faculdade de Engenharia da Universidade do Porto, Rua Dr. Roberto Frias, Porto, s/n 4200-465, Portugal.ppalma@fe.up.pt;3. Laboratory of Separation and Reaction Engineering, Departamento de Engenharia Química, Faculdade de Engenharia da Universidade do Porto, Rua Dr. Roberto Frias, Porto, s/n 4200-465, Portugal.;4. Faculdade de Ciências, Requinte, Dep. Química e Bioquímica, Universidade do Porto, Rua Campo Alegre 687, Porto, 4169-007, Portugal.;5. IBB–Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Av. Rovisco Pais, Lisboa, 1049-001, Portugal.;6. Department of Bioengineering, Instituto Superior Técnico, Lisboa, Portugal.;7. Department of Molecular Medicine, College of Medicine, University of South Florida, Tampa, FL, 33612, USA.;8. Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. |
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| Abstract: | Partition ratios of 8 free l-amino acids (Gln, Glu, His, Lys, Met, Ser, Thr, and Tyr) were measured in 10 different polymer/polymer aqueous two-phase systems containing 0.15?M NaCl in 0.01?M phosphate buffer, pH 7.4. The solute-specific coefficients representing the solute dipole/dipole, hydrogen-bonding and electrostatic interactions with the aqueous environment of the amino acids were determined by multiple linear regression analysis using a modified linear solvation energy relationship. The solute-specific coefficients determined in this study together with the solute-specific coefficients reported previously for amino acids with non-polar side-chains where used in a Quantitative Structure/Property Relationship analysis. It is shown that linear combinations of these solute-specific coefficients are correlated well with various physicochemical, structural, and biological properties of amino acids. |
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