Fluorine NMR of proteins

Using O 2 to probe membrane immersion depth by 19 F NMR

“…Fluorine NMR offers distinct advantages in the study of membrane protein structure (14)(15)(16)(17). In particular, sensitivity is nearly that obtained by 1 H, whereas the dispersion of chemical shifts is nearly 100-fold larger than that of 1 H. 19 F chemical shifts are also known to be very sensitive to local van der Waals and electrostatic environments.…”

Structural basis for the enhanced stability of highly fluorinated proteins

“…The introduction of fluorinated amino acids into proteins has attracted particular interest, because although essentially absent from biology, fluorine has proved a remarkably useful element to probe the workings of biological molecules. For example, fluorinated substrates have been extensively used to investigate enzyme mechanisms, and 19 F NMR has proved a valuable tool for studying structure, dynamics, and interactions of fluorine-labeled proteins, peptides, lipids, and nucleic acids (4)(5)(6)(7)(8)(9). Fluorinated molecules also have important medical applications, exemplified by 20% of all pharmaceuticals containing fluorine, which improves pharmacokinetic properties (10).…”

Notes on Synthesis of Perdeutero-5-13C,5,5,5-Trifluoroisoleucine VI56

“…Fluorine NMR spectroscopy is a powerful method for the study of both structure and dynamics of proteins and their interactions with other proteins or ligands [1][2][3][4]. Because of the ability of the 19 F lone-pair electrons to participate in non-bonded interactions with the local environment, 19 F chemical shifts are sensitive to changes in van der Waals contacts, electrostatic fields and hydrogen bonding.…”