Time-resolved IR studies of a variety of IR probes for studying local electrostatics and solvent structures in myoglobin, reverse micelles, and peptides
TRVS 2015
Summary:
Femtosecond infra-red spectroscopy, due to its inherent sub-picosecond resolution, has been extensively applied to studying ultrafast conformational changes and solvation phenomena in various molecular systems. To provide site-specific information on local electrostatic environment and solvation structure, small IR probes that act as antennae, sensing local electric field and hydrogen-bonding interactions, have been introduced into a variety of molecules, comprising the structure of peptides, proteins and nucleotides
Recently, we have developed new IR probes based on terminally-blocked isocyano(NC)-derivatized amino acids, i.e. β-isocyanoalanine and p-isocyanophenylalanine[5], which can be site-specifically introduced into both aliphatic and aromatic residues in proteins. Considering their unique properties including large intensity, exceptionally high sensitivity to hydrogen-bonding environment, and relatively long vibrational lifetime, we believe that such isonitrile non-natural amino acids will become very popular IR probes for studying ultrafast dynamics of biomolecules.
One eye-catching figure: