Applying γ‐Substituted Prolines in the Foldon Peptide: Polarity Contradicts Preorganization. Issue 3 (16th December 2014)

• Record Type: Journal Article
• Authors: Dietz, Dennis; Kubyshkin, Vladimir; Budisa, Nediljko
• Is Part Of: Chembiochem. Volume 16:Issue 3(2015)
• Page Start: 403
• Page End: 406
• Publication Date: 2014-12-16
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201402654
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Rational choice of chemical modifications to proline residues allows the preorganization principle to be exploited for more stable assembly of the <italic>foldon</italic> domain as a tag for trimerization. With systematic knowledge of how chemical and steric variations of the ring substituents affect the relative stabilities of <italic>exo</italic> and <italic>endo</italic> puckers, the preorganization principle should then be usable in biotechnologically synthesized <italic>foldon</italic> mutants and applicable for protein tagging elsewhere.</p> </abstract>