Applying γ-Substituted Prolines in the Foldon Peptide: Polarity Contradicts Preorganization

D. Dietz, V. Kubyshkin, N. Budisa. – 2015

Rational choice of chemical modifications to proline residues allows the preorganization principle to be exploited for more stable assembly of the foldon domain as a tag for trimerization. With systematic knowledge of how chemical and steric variations of the ring substituents affect the relative stabilities of exo and endo puckers, the preorganization principle should then be usable in biotechnologically synthesized foldon mutants and applicable for protein tagging elsewhere.

Titel
Applying γ-Substituted Prolines in the Foldon Peptide: Polarity Contradicts Preorganization
Verfasser
D. Dietz, V. Kubyshkin, N. Budisa.
Datum
2015
Kennung
10.1002/cbic.201402654
Zitierweise
ChemBioChem, 2015, 16, 403–406
Art
Text
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