@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.}
}
@article {2247,
	title = {Stabilization provided by neighboring strands is critical for the mechanical stability of proteins},
	journal = {Biophysical Journal},
	volume = {95},
	number = {8},
	year = {2008},
	note = {ISI Document Delivery No.: 352NMTimes Cited: 5Cited Reference Count: 37Sharma, Deepak Feng, Gang Khor, Dingyue Genchev, Georgi Z. Lu, Hui Li, Hongbin},
	month = {Oct},
	pages = {3935-3942},
	type = {Article},
	abstract = {Single-molecule force spectroscopy studies and steered molecular dynamics simulations have revealed that protein topology and pulling geometry play important roles in determining the mechanical stability of proteins. Most studies have focused on local interactions that are associated with the force-bearing beta-strands. Interactions mediated by neighboring strands are often overlooked. Here we use Top7 and barstar as model systems to illustrate the critical importance of the stabilization effect provided by neighboring beta-strands on the mechanical stability. Using single-molecule atomic force microscopy, we showed that Top7 and barstar, which have similar topology in their force-bearing region, exhibit vastly different mechanical-stability characteristics. Top7 is mechanically stable and unfolds at similar to 150 pN, whereas barstar is mechanically labile and unfolds largely below 50 pN. Steered molecular dynamics simulations revealed that stretching force peels one force-bearing strand away from barstar to trigger unfolding, whereas Top7 unfolds via a substructure-sliding mechanism. This previously overlooked stabilization effect from neighboring beta-strands is likely to be a general mechanism in protein mechanics and can serve as a guideline for the de novo design of proteins with significant mechanical stability and novel protein topology.},
	keywords = {BARSTAR, DYNAMICS SIMULATIONS, IMMUNOGLOBULIN DOMAINS, MICROSCOPE, MOLECULE FORCE SPECTROSCOPY, resistance, SINGLE PROTEIN, TITIN, TOPOLOGY, UBIQUITIN},
	isbn = {0006-3495},
	url = {<Go to ISI>://000259503900036},
	author = {Sharma, D. and Feng, G. and Khor, D. and Genchev, G. Z. and Lu, H. and Li, H. B.}
}
@article {3343,
	title = {PROTOTYPE FOR A NEW FAMILY OF DE-NOVO PROTEINS},
	journal = {Tetrahedron Letters},
	volume = {36},
	number = {42},
	year = {1995},
	note = {ISI Document Delivery No.: RZ295Times Cited: 24Cited Reference Count: 30},
	month = {Oct},
	pages = {7587-7590},
	type = {Article},
	abstract = {We report the design, synthesis, and preliminary structural analysis of a four-helix bundle affixed to a rigid organic macrocycle.},
	keywords = {ASSEMBLED SYNTHETIC PROTEINS, CAVITANDS, CHANNEL, DESIGN, HOST GUEST COMPLEXATION, MOLECULAR, PEPTIDE, TASP, TOPOLOGY, VESSELS},
	isbn = {0040-4039},
	url = {<Go to ISI>://A1995RZ29500004},
	author = {Gibb, B. C. and Mezo, A. R. and Sherman, J. C.}
}
