title: Residue-specific structural kinetics of proteins through the union of isotope labeling, mid-IR pulse shaping, and coherent 2D IR spectroscopy.
abstract: We describe a methodology for studying protein kinetics using a rapid-scan technology for collecting 2D IR spectra. In conjunction with isotope labeling, 2D IR spectroscopy is able to probe the secondary structure and environment of individual residues in polypeptides and proteins. It is particularly useful for membrane and aggregate proteins. Our rapid-scan technology relies on a mid-IR pulse shaper that computer generates the pulse shapes, much like in an NMR spectrometer. With this device, data collection is faster, easier, and more accurate. We describe our 2D IR spectrometer, as well as protocols for (13)C(18)O isotope labeling, and then illustrate the technique with an application to the aggregation of the human islet amyloid polypeptide implicated in type 2 diabetes.
authors.affiliation: Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706-1396, United States.
authors.forename: Chris T
authors.initials: CT
authors.lastname: Middleton
authors.forename: Ann Marie
authors.initials: AM
authors.lastname: Woys
authors.forename: Sudipta S
authors.initials: SS
authors.lastname: Mukherjee
authors.forename: Martin T
authors.initials: MT
authors.lastname: Zanni
mesh_terms: D000596:Amino Acids / Q000138:chemical synthesis; D000682:Amyloid / Q000737:chemistry; D002247:Carbon Isotopes; D006801:Humans; D007553:Isotope Labeling / Q000379:methods; D007700:Kinetics; D008565:Membrane Proteins / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D010103:Oxygen Isotopes; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013055:Spectrophotometry, Infrared / Q000295:instrumentation / Q000379:methods
chemical_list: D000596:Amino Acids; D000682:Amyloid; D002247:Carbon Isotopes; D008565:Membrane Proteins; D010103:Oxygen Isotopes; D011506:Proteins
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