Probing protein-protein interactions in real time

We have used a prototype small cantilever atomic force microscope to observe, in real time, the interactions between individual protein molecules. In particular, we have observed individual molecules of the chaperonin protein GroES binding to and then dissociating from individual GroEL proteins, whi...

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Published inNature structural & molecular biology Vol. 7; no. 8; pp. 644 - 647
Main Authors Viani, Mario B, Pietrasanta, Lia I, Thompson, James B, Chand, Ami, Gebeshuber, Ilse C, Kindt, Johannes H, Richter, Michael, Hansma, Helen G, Hansma, Paul K
Format Journal Article
LanguageEnglish
Published United States Nature Publishing Group 01.08.2000
Subjects
Aluminum Silicates
Chaperonin 10 - chemistry
Chaperonin 10 - metabolism
Chaperonin 10 - ultrastructure
Chaperonin 60 - chemistry
Chaperonin 60 - metabolism
Chaperonin 60 - ultrastructure
Escherichia coli
Microscopy, Atomic Force
Protein Binding
Time Factors
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Summary:We have used a prototype small cantilever atomic force microscope to observe, in real time, the interactions between individual protein molecules. In particular, we have observed individual molecules of the chaperonin protein GroES binding to and then dissociating from individual GroEL proteins, which were immobilized on a mica support. This work suggests that the small cantilever atomic force microscope is a useful tool for studying protein dynamics at the single molecule level.
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ISSN:1072-8368
1545-9993
2331-365X
1545-9985
DOI:10.1038/77936