title: Applying γ-substituted prolines in the foldon peptide: polarity contradicts preorganization.
abstract: 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.
authors.affiliation: Biocatalysis Group, Institute of Chemistry, Technical University of Berlin, Müller-Breslau-Strasse 10, 10623 Berlin (Germany).
authors.forename: Dennis
authors.initials: D
authors.lastname: Dietz
authors.forename: Vladimir
authors.initials: V
authors.lastname: Kubyshkin
authors.forename: Nediljko
authors.initials: N
authors.lastname: Budisa
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D005461:Fluorine / Q000737:chemistry; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000737:chemistry*; D011487:Protein Conformation; D015202:Protein Engineering; D017510:Protein Folding
chemical_list: D010455:Peptides; D005461:Fluorine; D011392:Proline
keywords: 19F NMR spectroscopy; conformation analysis; protein engineering; protein folding; self-assembly