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

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.

keywords

SOLVATOCHROMIC COMPARISON METHOD; AQUEOUS 2-PHASE SYSTEMS; PARTITION-COEFFICIENTS; DISORDERED PROTEIN; INTRINSIC DISORDER; SIDE-CHAINS; PI-STAR; BETA; DESCRIPTORS; THRESHOLDS

subject category

Biochemistry & Molecular Biology; Biophysics

authors

Madeira, PP; Bessa, A; Alvares-Ribeiro, L; Aires-Barros, MR; Rodrigues, AE; Uversky, VN; Zaslavsky, BY

our authors

acknowledgements

Financial support for this work was in part provided by national research grant PTDC/EQU-EQU/112812/2009 for which the authors are thankful. A. Bessa acknowledges the scholarship within the Project PTDC/EQU-EQU/112812/2009 from Fundacao para a Ciencia e a Tecnologia (FCT). P.P. Madeira acknowledges the financial support (Grant SFRH/BPD/45055/2008) from FCT.

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