Defining intrinsic hydrophobicity of amino acids’ side chains in random coil conformation. Reversed-phase liquid chromatography of designed synthetic peptides vs. random peptide data sets-Reference-Cited by-同舟云学术

Defining intrinsic hydrophobicity of amino acids’ side chains in random coil conformation. Reversed-phase liquid chromatography of designed synthetic peptides vs. random peptide data sets

Published:2011-09 Issue:37 Volume:1218 Page:6348-6355
ISSN:0021-9673
Container-title:Journal of Chromatography A
language:en
Short-container-title:Journal of Chromatography A

Author:

Shamshurin Dmitry,Spicer Vic,Krokhin Oleg V.

Funder

Natural Sciences and Engineering Research Council of Canada

Publisher

Elsevier BV

Subject

Organic Chemistry,General Medicine,Biochemistry,Analytical Chemistry

Reference24 articles.

1. Evaluation of methods for measuring amino acid hydrophobicities and interactions

2. Prediction of peptide retention times in high-pressure liquid chromatography on the basis of amino acid composition

3. 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

4. Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest-neighbor or conformational effects

5. Utility of Retention Prediction Model for Investigation of Peptide Separation Selectivity in Reversed-Phase Liquid Chromatography: Impact of Concentration of Trifluoroacetic Acid, Column Temperature, Gradient Slope and Type of Stationary Phase

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