Amino acid/water interactions study: a new amino acid scale

• Published in: Journal of biomolecular structure & dynamics Vol. 32; no. 6; pp. 959 - 968
• Main Authors: Madeira, Pedro P., Bessa, Ana, Álvares-Ribeiro, Luís, Raquel Aires-Barros, M., Rodrigues, Alírio E., Uversky, Vladimir N., Zaslavsky, Boris Y.
• Format: Journal Article
• Language: English
• Published: England Taylor & Francis 03.06.2014
• Subjects: amino acids; Amino Acids - chemistry; aqueous two-phase partitioning; biological activity; descriptors; Dextrans - chemistry; Hydrogen Bonding; Phosphates - chemistry; Polyethylene Glycols - chemistry; protein structure; Quantitative Structure-Activity Relationship; Regression Analysis; Sodium Chloride - chemistry; Static Electricity; Stereoisomerism; Water - chemistry
• ISSN: 0739-1102; 1538-0254
• DOI: 10.1080/07391102.2013.800994

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.