About: Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density

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About: Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density Goto Sponge NotDistinct Permalink

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scientific article published on 01 August 1989

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в серпні 1989 (uk) artículu científicu espublizáu n'agostu de 1989 (ast) scientific article published on 01 August 1989 (en)
publication date	wds:Q69723632-8124C316-EBDA-48E2-9DB5-7861E8D7C7C1
publication date	1989-08-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q69723632-2F62EDBC-E8DA-4843-A366-633E1D409BCA wds:Q69723632-36A84D50-BA27-4A8E-8A18-1F54D201913D wds:Q69723632-423713F9-6C42-4072-8A57-71517DC376E4 wds:Q69723632-50C2A59D-BCDC-4CC3-ADEB-9E6C5F92D388 wds:Q69723632-81A57D53-D811-47A7-B7D8-772496247F83
cites work	A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution Paracelsin; characterization by NMR spectroscopy and circular dichroism, and hemolytic properties of a peptaibol antibiotic from the cellulolytically active mold Trichoderma reesei. Part B Evaluation of advanced silica packings for the separation of biopolymers by high-performance liquid chromatography. III. Retention and selectivity of proteins and peptides in gradient elution on non-porous monodisperse 1.5-microns reversed-phase sil Structure of trichorzianine A IIIc, an antifungal peptide from Trichoderma harzianum Determination of thermodynamic parameters for the interaction of a lipid-binding peptide and insulin with a reversed-phase column
author name string	wds:Q69723632-733D74CA-5A13-496C-882C-D5F711AC3F9B wds:Q69723632-7F56F6DC-C65A-4976-AEAB-4915156FA342 wds:Q69723632-A8301191-80CC-4202-A0EE-623BE993148A wds:Q69723632-CB276372-9D56-4184-9658-05F09A7D0C7B
author name string	H Brückner M T Hearn K K Unger D K Lork
rdfs:label	Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density (en) Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density (nl)
skos:prefLabel	Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density (en) Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density (nl)
name	Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density (en) Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density (nl)
title	wds:Q69723632-C49DD795-E221-4779-9794-68BFA1F8BA58
title	Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density (en)
page(s)	wds:Q69723632-E57B16C9-E9E0-4D30-B1F4-E84D11387A62
page(s)	135-145
instance of	wds:Q69723632-727702BA-0B0F-4DD2-A144-A6FF63CA0955
instance of	scholarly article
PubMed ID	wds:Q69723632-5CA76D6F-B58D-4CEB-AADB-3260F88D1F16
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2777969
PubMed ID	2777969
volume	wds:Q69723632-E3712B50-E76F-4613-9AB3-5AC03DE41412
volume	476
DOI	wds:Q69723632-3E96EB16-874C-4C48-94F9-939C6D13F0AD
DOI	http://dx.doi.org/10.1016/S0021-9673(01)93863-4
DOI	10.1016/S0021-9673(01)93863-4
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q69723632
is cites work of	Temperature profiling of polypeptides in reversed-phase liquid chromatography. II. Monitoring of folding and stability of two-stranded alpha-helical coiled-coils Temperature profiling of polypeptides in reversed-phase liquid chromatography. I. Monitoring of dimerization and unfolding of amphipathic alpha-helical peptides High-performance liquid chromatography of amino acids, peptides and proteins. XCVIII. The influence of different displacer salts on the bandwidth properties of proteins separated by gradient elution anion-exchange chromatography High-performance liquid chromatography of amino acids, peptides and proteins High-performance liquid chromatography of amino acids, peptides and proteins. XCVII. The influence of the gradient elution mode and displacer salt type on the retention properties of closely related protein variants separated by high-performance ani High-performance liquid chromatography of amino acids, peptides and proteins Investigations into the chromatographic behavior of a doxorubicin-peptide conjugate Thermodynamic analysis of the interaction between proteins and solid surfaces: application to liquid chromatography Peptides High-performance liquid chromatographic resolution of (R, S)-α-alkyl-α-amino acids as diastereomeric derivatives
is cites work of	wds:Q78753264-04BF1F5E-EC95-4204-92DF-A045151E39F9 wds:Q78529957-A2964D04-18F5-4639-96B6-C5A91E302AD2 wds:Q62564425-04773E03-79A2-48E1-9D55-B1DD006BFF4E wds:Q34601784-EF8E4AE2-089C-4411-B4B4-2882F5C68202 wds:Q57222764-C96CEE33-9A55-4E32-A58B-52953D9410C8 wds:Q68345250-129F5324-971E-4A08-8238-BC4CEC2F654C wds:Q68363063-14FF5437-80F9-4ECD-9D85-FCE419F3E85C wds:Q78753268-4B762825-5821-40CC-8164-CD95F312EEF8 wds:Q57222757-4021BCED-1DEB-4383-9613-6808AE72FB9D wds:Q86645949-821303F5-4B16-4C0C-ADAC-C57778C91366

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