Journal
SCIENCE
Volume 323, Issue 5914, Pages 633-637Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1166191
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Funding
- Deutsche Forschungsgemeinschaft [RI 990/3-1]
- International Graduate School Materials Science of Complex Interfaces
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Single- molecule force spectroscopy allows superb mechanical control of protein conformation. We used a custom- built low- drift atomic force microscope to observe mechanically induced conformational equilibrium fluctuations of single molecules of the eukaryotic calcium- dependent signal transducer calmodulin ( CaM). From this data, the ligand dependence of the full energy landscape can be reconstructed. We find that calcium ions affect the folding kinetics of the individual CaM domains, whereas target peptides stabilize the already folded structure. Single- molecule data of full length CaM reveal that a wasp venom peptide binds noncooperatively to CaM with 2: 1 stoichiometry, whereas a target enzyme peptide binds cooperatively with 1: 1 stoichiometry. If mechanical load is applied directly to the target peptide, real- time binding/ unbinding transitions can be observed.
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