@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 = {://000258325800018}, author = {Cao, Y. and Li, H. B.} }