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, 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.
Viani
M B
MB
Department of Physics, University of California at Santa Barbara, Santa Barbara, California 93106, USA. viani@physics.ucsb.edu
Pietrasanta
L I
LI
Thompson
J B
JB
Chand
A
A
Gebeshuber
I C
IC
Kindt
J H
JH
Richter
M
M
Hansma
H G
HG
Hansma
P K
PK
D000538:Aluminum Silicates; D018835:Chaperonin 10 / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*; D004926:Escherichia coli; D018625:Microscopy, Atomic Force; D011485:Protein Binding; D013997:Time Factors
D000538:Aluminum Silicates; D018835:Chaperonin 10; D018834:Chaperonin 60; C011934:mica