TY - JOUR
T1 - Single protein misfolding events captured by atomic force microscopy
AU - Oberhauser, Andres F.
AU - Marszalek, Piotr E.
AU - Carrion-Vazquez, Mariano
AU - Fernandez, Julio M.
N1 - Funding Information:
We would like to thank H.P. Erickson (Duke University) for providing the human tenascin protein. This work was supported by NIH grants to J.M.F., P.E.M. and A.F.O.
PY - 1999
Y1 - 1999
N2 - Using single protein atomic force microscopy (AFM) techniques we demonstrate that after repeated mechanical extension/relaxation cycles, tandem modular proteins can misfold into a structure formed by two neighboring modules. The misfolding is fully reversible and alters the mechanical topology of the modules while it is about as stable as the original fold. Our results show that modular proteins can assume a novel misfolded state and demonstrate that AFM is able to capture, in real time, rare misfolding events at the level of a single protein.
AB - Using single protein atomic force microscopy (AFM) techniques we demonstrate that after repeated mechanical extension/relaxation cycles, tandem modular proteins can misfold into a structure formed by two neighboring modules. The misfolding is fully reversible and alters the mechanical topology of the modules while it is about as stable as the original fold. Our results show that modular proteins can assume a novel misfolded state and demonstrate that AFM is able to capture, in real time, rare misfolding events at the level of a single protein.
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U2 - 10.1038/14907
DO - 10.1038/14907
M3 - Article
C2 - 10542093
AN - SCOPUS:0032708281
VL - 6
SP - 1025
EP - 1028
JO - Nature Structural Biology
JF - Nature Structural Biology
SN - 1545-9993
IS - 11
ER -