Inference of the solvation energy parameters of amino acids using maximum entropy approach.
We present a novel technique, based on the principle of maximum entropy, for deriving the solvation energy parameters of amino acids from the knowledge of the solvent accessible areas in experimentally determined native state structures as well as high quality decoys of proteins. We present the results of detailed studies and analyze the correlations of the solvation energy parameters with the standard hydrophobic scale. We study the ability of the inferred parameters to discriminate between the native state structures of proteins and their decoy conformations.
Hoang
Trinh X
TX
Physics Department, Penn State University, 104 Davey Lab, University Park, Pennsylvania 16801, USA.
Seno
Flavio
F
Trovato
Antonio
A
Banavar
Jayanth R
JR
Maritan
Amos
A
D000596:Amino Acids / Q000737:chemistry*; D019277:Entropy; D057927:Hydrophobic and Hydrophilic Interactions; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D012997:Solvents / Q000737:chemistry*; D013499:Surface Properties
D000596:Amino Acids; D011506:Proteins; D012997:Solvents