Force spectroscopy is a set of techniques for the study of the interactions and the binding forces between individual molecules.[1][2] These methods can be used to measure the mechanical properties of single polymermolecules or proteins, or individual chemical bonds. The name "force spectroscopy", although widely used in the scientific community, is somewhat misleading, because there is no true matter-radiation interaction.[3]
Force spectroscopy measures the behavior of a molecule under stretching or torsional mechanical force. In this way a great deal has been learned in recent years about the mechanochemical coupling in the enzymes responsible for muscle contraction, transport in the cell, energy generation (F1-ATPase), DNA replication and transcription (polymerases), DNA unknotting and unwinding (topoisomerases and helicases).[8]
As a single-molecule technique, as opposed to typical ensemble spectroscopies, it allows a researcher to determine properties of the particular molecule under study. In particular, rare events such as conformational change, which are masked in an ensemble, may be observed.
^ abHoffmann T, Dougan L (July 2012). "Single molecule force spectroscopy using polyproteins". Chemical Society Reviews. 41 (14): 4781–4796. doi:10.1039/c2cs35033e. PMID22648310.