Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: Comparison with other hydrophilicity/hydrophobicity scales
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/bip.21316/fullpdf
Reference51 articles.
1. Quantitative comparison of the ability of hydropathy scales to recognize surface ?-strands in proteins
2. Evaluation of methods for measuring amino acid hydrophobicities and interactions
3. Predictions of peptides' retention times in reversed-phase liquid chromatography as a new supportive tool to improve protein identification in proteomics
4. Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest-neighbor or conformational effects
5. Requirements for prediction of peptide retention time in reversed-phase high-performance liquid chromatography: Hydrophilicity/hydrophobicity of side-chains at the N- and C-termini of peptides are dramatically affected by the end-groups and location
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