Proceedings of the National Academy of Sciences - PNAS, 1999-08, Vol.96 (18), p.10115-10117
1999
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Details
- Autor(en) / Beteiligte
- Titel
- Compactness of the Denatured State of a Fast-Folding Protein Measured by Submillisecond Small-Angle X-Ray Scattering
- Ist Teil von
- Proceedings of the National Academy of Sciences - PNAS, 1999-08, Vol.96 (18), p.10115-10117
- Ort / Verlag
- United States: National Academy of Sciences of the United States of America
- Erscheinungsjahr
- 1999
- Quelle
- Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
- Beschreibungen/Notizen
- Time-resolved small-angle x-ray scattering was used to measure the radius of gyration of cytochrome c after initiation of folding by a pH jump. Submillisecond time resolution was obtained with a microfabricated diffusional mixer and synchrotron radiation. The results show that the protein first collapses to compact denatured structures before folding very fast to the native state.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0027-8424eISSN: 1091-6490DOI: 10.1073/pnas.96.18.10115Titel-ID: cdi_pnas_primary_96_18_10115
- Format
- –
- Schlagworte
- Biological Sciences, Crystallography, X-Ray - instrumentation, Crystallography, X-Ray - methods, Cytochrome c Group - chemistry, Cytochrome c Group - metabolism, Cytochromes, Fluorescence, Gyration, Hydrogen-Ion Concentration, Kinetics, Narrative devices, Protein Denaturation, Protein Folding, Proteins, Synchrotron radiation, Time Factors, Topological compactness, Topology, X-rays