@article {2033,
	title = {Engineered elastomeric proteins with dual elasticity can be controlled by a molecular regulator},
	journal = {Nature Nanotechnology},
	volume = {3},
	number = {8},
	year = {2008},
	note = {ISI Document Delivery No.: 335WZTimes Cited: 12Cited Reference Count: 29Cao, Yi Li, Hongbin},
	month = {Aug},
	pages = {512-516},
	type = {Article},
	abstract = {Elastomeric proteins are molecular springs that confer excellent mechanical properties(1-5) to many biological tissues and biomaterials. Depending on the role performed by the tissue or biomaterial, elastomeric proteins can behave as molecular springs(1,2,6,7) or shock absorbers(3-5,8-10). Here we combine single-molecule atomic force microscopy and protein engineering techniques to create elastomeric proteins that can switch between two distinct types of mechanical behaviour in response to the binding of a molecular regulator. The proteins are mechanically labile by design and behave as entropic springs with an elasticity that is governed by their configurational entropy. However, when a molecular regulator binds to the protein, it switches into a mechanically stable state and can act as a shock absorber. These engineered proteins effectively mimic and combine the two extreme forms of elastic behaviour found in natural elastomeric proteins, and thus represent a new type of smart nanomaterial that will find potential applications in nanomechanics and material sciences.},
	keywords = {BINDING, BIOLOGICAL ROLES, DESIGN, DOMAINS, FORCE-SPECTROSCOPY, MECHANICAL-PROPERTIES, STABILITY, TITINS, TOPOLOGY},
	isbn = {1748-3387},
	url = {<Go to ISI>://000258325800018},
	author = {Cao, Y. and Li, H. B.}
}
