TY - JOUR
T1 - The study of protein mechanics with the atomic force microscope
AU - Fisher, Thomas E.
AU - Oberhauser, Andres F.
AU - Carrion-Vazquez, Mariano
AU - Marszalek, Piotr E.
AU - Fernandez, Julio M.
N1 - Funding Information:
This work was funded by R01 grants from the National Institutes of Health to J. M. Fernandez.
PY - 1999/10/1
Y1 - 1999/10/1
N2 - The unfolding and folding of single protein molecules can be studied with an atomic force microscope (AFM). Many proteins with mechanical functions contain multiple, individually folded domains with similar structures. Protein engineering techniques have enabled the construction and expression of recombinant proteins that contain multiple copies of identical domains. Thus, the AFM in combination with protein engineering has enabled the kinetic analysis of the force-induced unfolding and refolding of individual domains as well as the study of the determinants of mechanical stability. Copyright (C) 1999 Elsevier Science Ltd.
AB - The unfolding and folding of single protein molecules can be studied with an atomic force microscope (AFM). Many proteins with mechanical functions contain multiple, individually folded domains with similar structures. Protein engineering techniques have enabled the construction and expression of recombinant proteins that contain multiple copies of identical domains. Thus, the AFM in combination with protein engineering has enabled the kinetic analysis of the force-induced unfolding and refolding of individual domains as well as the study of the determinants of mechanical stability. Copyright (C) 1999 Elsevier Science Ltd.
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U2 - 10.1016/S0968-0004(99)01453-X
DO - 10.1016/S0968-0004(99)01453-X
M3 - Review article
C2 - 10500301
AN - SCOPUS:0033214502
SN - 0968-0004
VL - 24
SP - 379
EP - 384
JO - Trends in biochemical sciences
JF - Trends in biochemical sciences
IS - 10
ER -