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-Reference-Cited by-同舟云学术

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

Published:2009 Issue:6 Volume:92 Page:573-595
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Mant Colin T.,Kovacs James M.,Kim Hyun-Min,Pollock David D.,Hodges Robert S.

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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