title: Isotope-edited infrared spectroscopy.
abstract: Isotope-edited infrared (IR) spectroscopy is a powerful tool for studying structural and dynamical properties of peptides and proteins with site-specific resolution. Labeling of selected amide carbonyls with (13)C results in detectable sidebands of amide I' vibrations, which provide information about local conformation and/or solvent exposure without structural perturbation to the protein. Incorporation of isotopically labeled amino acids at specific positions is achieved by the chemical synthesis of the studied proteins. We describe the basic procedures for synthesis of (13)C isotopically edited protein samples, experimental IR spectroscopic measurements, and analysis of the site-specific structural changes from the thermal unfolding IR data.
authors: Department of Chemistry, University of Wyoming, Laramie, WY, USA.
authors: Ginka S
authors: GS
authors: Buchner
authors: Jan
authors: J
authors: Kubelka
mesh_terms: D000465:Algorithms; D000596:Amino Acids / Q000737:chemistry; D002247:Carbon Isotopes; D005449:Fluorenes / Q000737:chemistry; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D044367:Phase Transition; D017434:Protein Structure, Tertiary; D058767:Protein Unfolding; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D000596:Amino Acids; D002247:Carbon Isotopes; D005449:Fluorenes; C016456:N(alpha)-fluorenylmethyloxycarbonylamino acids; D010455:Peptides