NMR Spectroscopy of supramolecular chemistry on protein surfaces

• Peter Bayer,
• Anja Matena and
• Christine Beuck

Beilstein J. Org. Chem. 2020, 16, 2505–2522, doi:10.3762/bjoc.16.203

• modulate protein–protein interactions. Here we present NMR methods that have been applied to characterize these molecular interactions and discuss the challenges of this endeavor. Keywords: molecular recognition; NMR; protein ligand interaction; protein surfaces; supramolecular chemistry; Introduction In

Synthesis of fluorinated maltose derivatives for monitoring protein interaction by ¹⁹F NMR

• Michaela Braitsch,
• Hanspeter Kählig,
• Georg Kontaxis,
• Michael Fischer,
• Toshinari Kawada,
• Robert Konrat and
• Walther Schmid

Beilstein J. Org. Chem. 2012, 8, 448–455, doi:10.3762/bjoc.8.51

• studies of protein–ligand interaction interfaces. Keywords: fluorination; 19F NMR; maltose-binding protein (MBP); maltose derivatives; protein interaction; Introduction In recent years, we have witnessed significant improvements in NMR spectroscopy, especially as a powerful tool for studying protein

• , the different binding affinities of selectively 19F-labeled maltose derivatives to MBP illustrate how the recently established correlation between 19F chemical shift data and molecular interaction patterns [48][49] can be used to delineate details of protein–ligand interaction interfaces. Together

Chemical aminoacylation of tRNAs with fluorinated amino acids for in vitro protein mutagenesis

• Shijie Ye,
• Allison Ann Berger,
• Dominique Petzold,
• Oliver Reimann,
• Benjamin Matt and
• Beate Koksch

Beilstein J. Org. Chem. 2010, 6, No. 40, doi:10.3762/bjoc.6.40

• atoms within the peptide chain [17][18][19]. Finally, due to the high NMR sensitivity of fluorine, the incorporation of fluorinated amino acid analogues into proteins provides the opportunity for probing the structure and dynamics that play a role in protein–protein and protein–ligand interaction, and