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000055022 0247_ $$2DOI$$a10.1002/elps.200500673
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000055022 084__ $$2WoS$$aBiochemical Research Methods
000055022 084__ $$2WoS$$aChemistry, Analytical
000055022 1001_ $$0P:(DE-HGF)0$$aPsurek, A.$$b0
000055022 245__ $$aNonaqueous versus aqueous capillary electrophoresis of alpha-helical polypeptides: Effect of secondary structure on separation selectivity
000055022 260__ $$aWeinheim$$bWiley-Blackwell$$c2006
000055022 300__ $$a1768 - 1775
000055022 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000055022 440_0 $$01792$$aElectrophoresis$$v27$$x0173-0835$$y9
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000055022 520__ $$aThe CE separation of alpha-helical polypeptides composed of 14-31 amino acid residues has been investigated using aqueous and nonaqueous BGEs. The running buffers were optimized with respect to pH. Generally, higher separation selectivities were observed in nonaqueous electrolytes. This may be explained by a change in the secondary structure when changing from water to organic solvents. Circular dichroism spectra revealed a significant increase in helical structures in methanol-based buffers compared to aqueous buffers. This change in secondary structure of the polypeptides contributed primarily to the different separation selectivity observed in aqueous CE and NACE. For small oligopeptides of two to five amino acid residues no significant effect of the solvent was observed in some cases while in other cases a reversal of the migration order occurred when changing from aqueous to nonaqueous buffers. As these peptides cannot adopt secondary structures the effect may be attributed to a shift of the pKa values in organic solvents compared to water.
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000055022 588__ $$aDataset connected to Web of Science, Pubmed
000055022 650_2 $$2MeSH$$aAmino Acid Sequence
000055022 650_2 $$2MeSH$$aCircular Dichroism
000055022 650_2 $$2MeSH$$aElectrophoresis, Capillary: methods
000055022 650_2 $$2MeSH$$aMolecular Sequence Data
000055022 650_2 $$2MeSH$$aPeptides: chemistry
000055022 650_2 $$2MeSH$$aPeptides: isolation & purification
000055022 650_2 $$2MeSH$$aProtein Structure, Secondary
000055022 650_2 $$2MeSH$$aWater: chemistry
000055022 650_7 $$00$$2NLM Chemicals$$aPeptides
000055022 650_7 $$07732-18-5$$2NLM Chemicals$$aWater
000055022 650_7 $$2WoSType$$aJ
000055022 65320 $$2Author$$acircular dichroism spectroscopy
000055022 65320 $$2Author$$aalpha-Helical pepticles
000055022 65320 $$2Author$$anonaqueous capillary electrophoresis
000055022 65320 $$2Author$$asecondary structure
000055022 7001_ $$0P:(DE-Juel1)VDB89238$$aFeuerstein, S.E.$$b1$$uFZJ
000055022 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b2$$uFZJ
000055022 7001_ $$0P:(DE-HGF)0$$aScriba, G. K. E.$$b3
000055022 773__ $$0PERI:(DE-600)1475486-1$$a10.1002/elps.200500673$$gVol. 27, p. 1768 - 1775$$p1768 - 1775$$q27<1768 - 1775$$tElectrophoresis$$v27$$x0173-0835$$y2006
000055022 8567_ $$uhttp://dx.doi.org/10.1002/elps.200500673
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000055022 9141_ $$y2006
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000055022 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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