title: Deconstructing time-resolved optical rotatory dispersion kinetic measurements of cytochrome c folding: from molten globule to the native state.
abstract: The far-UV time-resolved optical rotatory dispersion (TRORD) technique has contributed significantly to our understanding of nanosecond secondary structure kinetics in protein folding and function reactions. For reduced cytochrome c, protein folding kinetics have been probed largely from the unfolded to the native state. Here we provide details about sample preparation and the TRORD apparatus and measurements for studying folding from a partly unfolded state to the native secondary structure conformation of reduced cytochrome c.
authors: Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA, USA. chen@chemistry.ucsc.edu
authors: Eefei
authors: E
authors: Chen
authors: David S
authors: DS
authors: Kliger
mesh_terms: D002942:Circular Dichroism; D045304:Cytochromes c / Q000737:chemistry*; D007700:Kinetics; D044367:Phase Transition; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry; D013501:Surface-Active Agents / Q000737:chemistry; D017186:Titrimetry
chemical_list: D013501:Surface-Active Agents; D012967:Sodium Dodecyl Sulfate; D045304:Cytochromes c