title: Studying biomacromolecules with two-dimensional infrared spectroscopy.
abstract: Two-dimensional infrared (2DIR) spectroscopy is a rapidly developing nonlinear spectroscopy, which allows access to greater structural detail than traditional vibrational spectroscopies. The ability to gain extra structural insight is particularly relevant to the study of biomacromolecules, whose Fourier transform infrared (FTIR) spectra are often congested, due to the large number of vibrations. The subpicosecond timescale of the spectroscopy gives the opportunity to follow the fluctuations of a molecule in the time domain. Theoretical and experimental techniques are well developed for 2DIR, and they have already given insight into some of the fundamental aspects of the structure and dynamics of proteins and nucleic acids. This chapter reviews some of these recent studies and showcases the potential of the method.
authors.affiliation: School of Chemistry, University of Nottingham, University Park, Nottingham, United Kingdom.
authors.forename: Rachel E
authors.initials: RE
authors.lastname: Hill
authors.forename: Neil T
authors.initials: NT
authors.lastname: Hunt
authors.forename: Jonathan D
authors.initials: JD
authors.lastname: Hirst
mesh_terms: D006860:Hydrogen Bonding; D009696:Nucleic Acids; D011506:Proteins / Q000737:chemistry; D013055:Spectrophotometry, Infrared; D014732:Vibration
chemical_list: D009696:Nucleic Acids; D011506:Proteins
keywords: Biomacromolecules; Nucleic acids; Proteins; Two-dimensional Infrared; Ultrafast