Investigations of Biomolecular Conformation and Dynamics using 19F NMR
Pp. 116-149 (34)
Fluorine NMR is a useful probe of protein structure, conformation and
folding in fluorinated proteins, owing to the high sensitivity, large chemical shift of the
19F nucleus and the lack of high background signal to be suppressed. Protein NMR
studies using fluorinated amino acids are a valuable addition to the existing suite of
experiments with isotopically enriched nuclei. Recently, there have been several efforts
to develop novel methods of biosynthetically tagging proteins to contain 19F labels
using fluorinated amino acids. Each fluorine signal in the resultant protein then
becomes a reporter of the protein’s structure and conformational dynamics. 19F NMR
relaxation times (including T1 relaxation and homonuclear and heteronuclear NOE
relaxation) can give detailed structural information. The 19F CSA mechanism is an
important relaxation mechanism at high magnetic fields and several novel experiments
have been designed, to determine the complete 19F CSA tensor. Several groups are also
trying to apply 19F NMR techniques to study membrane proteins and intrinsically
disordered proteins which have a fluorinated tag. This chapter will focus on novel
NMR techniques using fluorine as a probe and their application to structure
determination and conformational dynamics of fluorinated biomolecules.
Biomolecular conformation, Biomolecular dynamics, Fluorinated
amino acids, Fluorine spin, Multidimensional NMR.
Department of Physical Sciences, Indian Institute of Science Education & Research (IISER) Mohali, Sector 81 Mohali, Punjab 160062, India.