About: Monitoring the hydrophilicity/hydrophobicity of amino acid side-chains in the non-polar and polar faces of amphipathic alpha-helices by reversed-phase and hydrophilic interaction/cation-exchange chromatography

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About: Monitoring the hydrophilicity/hydrophobicity of amino acid side-chains in the non-polar and polar faces of amphipathic alpha-helices by reversed-phase and hydrophilic interaction/cation-exchange chromatography Goto Sponge NotDistinct Permalink

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scientific article published on 01 October 2004

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 2004 (uk) artículu científicu espublizáu n'ochobre de 2004 (ast) scientific article published on 01 October 2004 (en)
publication date	wds:Q81007814-1AC2A38E-E8C4-4914-87C6-DE6EEBC9EFD5
publication date	2004-10-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q81007814-0FE9DFBF-28B3-45F4-9181-AE580C17BDE6 wds:Q81007814-2B573C14-9FC5-4995-930B-C94CA09FF593 wds:Q81007814-76978B15-6945-4134-9988-82FCED416A5E wds:Q81007814-831BAEB4-3F1D-44AF-A836-5E9140A97057
author name string	Y Chen R S Hodges C T Mant E Kopecky
rdfs:label	Monitoring the hydrophilicity/hydrophobicity of amino acid side-chains in the non-polar and polar faces of amphipathic alpha-helices by reversed-phase and hydrophilic interaction/cation-exchange chromatography (en) Monitoring the hydrophilicity/hydrophobicity of amino acid side-chains in the non-polar and polar faces of amphipathic alpha-helices by reversed-phase and hydrophilic interaction/cation-exchange chromatography (nl)
skos:prefLabel	Monitoring the hydrophilicity/hydrophobicity of amino acid side-chains in the non-polar and polar faces of amphipathic alpha-helices by reversed-phase and hydrophilic interaction/cation-exchange chromatography (en) Monitoring the hydrophilicity/hydrophobicity of amino acid side-chains in the non-polar and polar faces of amphipathic alpha-helices by reversed-phase and hydrophilic interaction/cation-exchange chromatography (nl)
name	Monitoring the hydrophilicity/hydrophobicity of amino acid side-chains in the non-polar and polar faces of amphipathic alpha-helices by reversed-phase and hydrophilic interaction/cation-exchange chromatography (en) Monitoring the hydrophilicity/hydrophobicity of amino acid side-chains in the non-polar and polar faces of amphipathic alpha-helices by reversed-phase and hydrophilic interaction/cation-exchange chromatography (nl)
title	wds:Q81007814-9D61368D-C531-4F8B-8810-55CD7D4F80D3
title	Monitoring the hydrophilicity/hydrophobicity of amino acid side-chains in the non-polar and polar faces of amphipathic alpha-helices by reversed-phase and hydrophilic interaction/cation-exchange chromatography (en)
page(s)	wds:Q81007814-6881EAC1-49FD-4FDC-B7CF-8B189B0FA443
page(s)	161-172
instance of	wds:Q81007814-CE02753F-8099-45CB-9E48-B2BF2B6983B6
instance of	scholarly article
PubMed ID	wds:Q81007814-AEA5ED27-5E58-4873-9DAB-C46C48E79915
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/15543982
PubMed ID	15543982
published in	wds:Q81007814-A50C4BD7-E8C6-42A4-BC01-6738B672FE43
published in	Journal of Chromatography
issue	wds:Q81007814-2CBDA455-2E13-4E63-BBC6-066FEC8A2E4E
volume	wds:Q81007814-28FB7865-AC4B-489A-B8C0-7070D52E076C
issue	1-2
volume	1053
number of pages	wds:Q81007814-6330B03E-83B7-4DE2-9B95-47E66A793B19
number of pages	12 (xsd:decimal)
DOI	wds:Q81007814-EE0F5775-4FA6-41B6-A83B-5F89591E4BB9
DOI	http://dx.doi.org/10.1016/S0021-9673(04)01496-7
DOI	10.1016/S0021-9673(04)01496-7
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q81007814
is cites work of	De novo designed synthetic mimics of antimicrobial peptides Mixed-mode hydrophilic interaction/cation-exchange chromatography (HILIC/CEX) of peptides and proteins Ion-interaction CZE: the presence of high concentrations of ion-pairing reagents demonstrates the complex mechanisms involved in peptide separations HPLC analysis and purification of peptides HPLC Analysis and Purification of Peptides Mixed-mode hydrophilic interaction/cation-exchange chromatography: separation of complex mixtures of peptides of varying charge and hydrophobicity Structure-guided RP-HPLC chromatography of diastereomeric α-helical peptide analogs substituted with single amino acid stereoisomers
is cites work of	wds:Q37321460-3282B514-5AAB-43DB-B688-32AE51D1B881 wds:Q44276923-4F0740B9-A3DC-4F24-8B52-5A2623DA97A2 wds:Q37231113-F7FA90E6-ECE5-4BBA-B0AA-EAE5F9108D82 wds:Q41789535-504415BA-5C84-423F-AB3D-CB5AA4BC30F8 wds:Q41899451-D4AD7589-9B9E-49C3-B76A-BBC6DE9F9F99 wds:Q56483985-AE439B60-5C77-4E32-AA07-AECB3A000838 wds:Q35017565-2377C175-1494-41F2-A563-98B489DEA9B3

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