title: Site-specific infrared probes of proteins.
abstract: Infrared spectroscopy has played an instrumental role in the study of a wide variety of biological questions. However, in many cases, it is impossible or difficult to rely on the intrinsic vibrational modes of biological molecules of interest, such as proteins, to reveal structural and environmental information in a site-specific manner. To overcome this limitation, investigators have dedicated many recent efforts to the development and application of various extrinsic vibrational probes that can be incorporated into biological molecules and used to site-specifically interrogate their structural or environmental properties. In this review, we highlight recent advancements in this rapidly growing research area.
authors.affiliation: Ultrafast Optical Processes Laboratory.
authors.forename: Jianqiang
authors.initials: J
authors.lastname: Ma
authors.forename: Ileana M
authors.initials: IM
authors.lastname: Pazos
authors.forename: Wenkai
authors.initials: W
authors.lastname: Zhang
authors.forename: Robert M
authors.initials: RM
authors.lastname: Culik
authors.forename: Feng
authors.initials: F
authors.lastname: Gai
mesh_terms: D000818:Animals; D006801:Humans; D008958:Models, Molecular; D015335:Molecular Probes / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013055:Spectrophotometry, Infrared / Q000379:methods*
chemical_list: D015335:Molecular Probes; D011506:Proteins
keywords: infrared spectroscopy; isotope editing; site-specific probe; unnatural amino acid; vibrational Stark effect spectroscopy; vibrational coupling