Journal
SCIENCE
Volume 334, Issue 6055, Pages 512-516Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1207598
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- Deutsche Forschungsgemeinschaft through Institute for Advanced Study of Technische Universitat Munchen [SFB 863 A2]
- International Graduate School Materials Science of Complex Interfaces
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Direct observation of the detailed conformational fluctuations of a single protein molecule en route to its folded state has so far been realized only in silico. We have used single-molecule force spectroscopy to study the folding transitions of single calmodulin molecules. High-resolution optical tweezers assays in combination with hidden Markov analysis reveal a complex network of on- and off-pathway intermediates. Cooperative and anticooperative interactions across domain boundaries can be observed directly. The folding network involves four intermediates. Two off-pathway intermediates exhibit non-native interdomain interactions and compete with the ultrafast productive folding pathway.
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