001     55022
005     20200402210300.0
024 7 _ |2 pmid
|a pmid:16645940
024 7 _ |2 DOI
|a 10.1002/elps.200500673
024 7 _ |2 WOS
|a WOS:000237685600011
037 _ _ |a PreJuSER-55022
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemical Research Methods
084 _ _ |2 WoS
|a Chemistry, Analytical
100 1 _ |a Psurek, A.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Nonaqueous versus aqueous capillary electrophoresis of alpha-helical polypeptides: Effect of secondary structure on separation selectivity
260 _ _ |a Weinheim
|b Wiley-Blackwell
|c 2006
300 _ _ |a 1768 - 1775
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Electrophoresis
|x 0173-0835
|0 1792
|y 9
|v 27
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The 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.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Circular Dichroism
650 _ 2 |2 MeSH
|a Electrophoresis, Capillary: methods
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Peptides: chemistry
650 _ 2 |2 MeSH
|a Peptides: isolation & purification
650 _ 2 |2 MeSH
|a Protein Structure, Secondary
650 _ 2 |2 MeSH
|a Water: chemistry
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptides
650 _ 7 |0 7732-18-5
|2 NLM Chemicals
|a Water
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a circular dichroism spectroscopy
653 2 0 |2 Author
|a alpha-Helical pepticles
653 2 0 |2 Author
|a nonaqueous capillary electrophoresis
653 2 0 |2 Author
|a secondary structure
700 1 _ |a Feuerstein, S.E.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB89238
700 1 _ |a Willbold, D.
|b 2
|u FZJ
|0 P:(DE-Juel1)132029
700 1 _ |a Scriba, G. K. E.
|b 3
|0 P:(DE-HGF)0
773 _ _ |a 10.1002/elps.200500673
|g Vol. 27, p. 1768 - 1775
|p 1768 - 1775
|q 27<1768 - 1775
|0 PERI:(DE-600)1475486-1
|t Electrophoresis
|v 27
|y 2006
|x 0173-0835
856 7 _ |u http://dx.doi.org/10.1002/elps.200500673
909 C O |o oai:juser.fz-juelich.de:55022
|p VDB
913 1 _ |k P33
|v Funktion und Dysfunktion des Nervensystems
|l Funktion und Dysfunktion des Nervensystems
|b Gesundheit
|0 G:(DE-Juel1)FUEK409
|x 0
914 1 _ |y 2006
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB58
|x 0
970 _ _ |a VDB:(DE-Juel1)85881
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)ICS-6-20110106


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