Force-clamp AFM, with its remarkable ability to manipulate short recombinant proteins, has become a useful probe of protein dynamics, allowing us to sense conformational changes down to the sub-Angstrom scale. The single protein data is providing a new view that will help guide the development of theories on enzyme catalysis, the statistical dynamics of folding, and ab initio studies of a chemical reaction while placed under a stretching force; of common occurrence in nature.
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Columbia Univ, Dept Biol Sci, New York, NY 10027 USAColumbia Univ, Dept Biol Sci, New York, NY 10027 USA
Popa, Ionel
Kosuri, Pallav
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Columbia Univ, Dept Biol Sci, New York, NY 10027 USAColumbia Univ, Dept Biol Sci, New York, NY 10027 USA
Kosuri, Pallav
Alegre-Cebollada, Jorge
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Columbia Univ, Dept Biol Sci, New York, NY 10027 USAColumbia Univ, Dept Biol Sci, New York, NY 10027 USA
Alegre-Cebollada, Jorge
Garcia-Manyes, Sergi
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Kings Coll London, Dept Phys, London WC2R 2LS, England
Kings Coll London, Randall Div Cell & Mol Biophys, London WC2R 2LS, EnglandColumbia Univ, Dept Biol Sci, New York, NY 10027 USA
Garcia-Manyes, Sergi
Fernandez, Julio M.
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Columbia Univ, Dept Biol Sci, New York, NY 10027 USAColumbia Univ, Dept Biol Sci, New York, NY 10027 USA