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Stereochemistry Rules: A Single Stereocenter Changes the Conformation of a Cyclic Tetrapeptide

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons101523

Bravo-Rodriguez,  Kenny
Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons58744

Lehmann,  Christian W.
Service Department Lehmann (EMR), Max-Planck-Institut für Kohlenforschung, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons101503

Sanchez-Garcia,  Elsa
Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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jp406497r_si_001.pdf
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Zitation

Li, F., Bravo-Rodriguez, K., Fernandez-Oliva, M., Ramirez-Anguita, J. M., Merz, K., Winter, M., et al. (2013). Stereochemistry Rules: A Single Stereocenter Changes the Conformation of a Cyclic Tetrapeptide. The Journal of Physical Chemistry B, 117(37), 10785-10791. doi:10.1021/jp406497r.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0014-A2C3-0
Zusammenfassung
Two novel cyclo(Boc-Cys-Pro-Leu-Cys-OMe) peptides 1 and 2 containing the enantiomeric amino acids D-Leu and L-Leu, respectively, were synthesized to investigate the effect of chiral centers on peptide conformations. By combining a variety of experimental techniques (X-ray crystallography, 2D NMR spectroscopy, temperaturedependent 1H NMR and IR spectroscopy, and UV-CD spectroscopy) with replica exchange molecular dynamics (REMD) techniques and quantum mechanics/molecular dynamics (QM/MM) calculations, we establish that the stereochemistry of just one residue can noticeably influence the properties of the whole peptide and rationalize the origins of this effect, with potential implications for the rational design of peptides of chemical and biological relevance.