The study of protein mechanics with the atomic force microscope

Citation
Te. Fisher et al., The study of protein mechanics with the atomic force microscope, TRENDS BIOC, 24(10), 1999, pp. 379-384
Citations number
39
Categorie Soggetti
Biochemistry & Biophysics
Journal title
TRENDS IN BIOCHEMICAL SCIENCES
ISSN journal
09680004 → ACNP
Volume
24
Issue
10
Year of publication
1999
Pages
379 - 384
Database
ISI
SICI code
0968-0004(199910)24:10<379:TSOPMW>2.0.ZU;2-V
Abstract
The unfolding and folding of single protein molecules can be studied with a n atomic force microscope (AFM). Many proteins with mechanical functions co ntain multiple, individually folded domains with similar structures. Protei n engineering techniques have enabled the construction and expression of re combinant proteins that contain multiple copies of identical domains. Thus, the AFM in combination with protein engineering has enabled the kinetic an alysis of the force-induced unfolding and refolding of individual domains a s well as the study of the determinants of mechanical stability.