ISSN:
0173-0835
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
On capillary electrophoresis of the chemically pure thioxo peptide Ala-Phe-ψ[CS-N]-Pro-Phe-4-nitroanilide a peak splitting was observed at a capillary temperature of 25°C. By contrast, the oxo peptide analogue exhibits a single, sharp peak under these conditions. Both peaks of the thioxo compound coincided gradually when the temperature was increased to 60°C. Peak fusion was reverted by cooling down the heated sample. This behavior could be attributed to the electrophoresis-mediated separation of the cis/trans prolyl bond isomers of the thioxo peptide, allowing data of this conformational equilibrium to be determined. Derived from computational data about molecular volume and the hydration energy of low-energy cis and trans isomeric structures, the more rapid migration of the cis form in comparison to trans may be explained by structural parameters.
Additional Material:
9 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/elps.11501501174
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