@article {2148,
	title = {{\textquoteright}Mechanical Engineering{\textquoteright} of Elastomeric Proteins: Toward Designing New Protein Building Blocks for Biomaterials},
	journal = {Advanced Functional Materials},
	volume = {18},
	number = {18},
	year = {2008},
	note = {ISI Document Delivery No.: 358QQTimes Cited: 6Cited Reference Count: 102Li, Hongbin},
	month = {Sep},
	pages = {2643-2657},
	type = {Review},
	abstract = {Elastomeric proteins are subject to stretching force under biological settings and play important roles in regulating the mechanical properties of a wide range of biological machinery. Elastomeric proteins also underlie the superb mechanical properties of many protein-based biomaterials. The developments of single molecule force spectroscopy have enabled the direct characterization of the mechanical properties of elastomeric proteins at the single molecule level and led to the new burgeoning field of research: single protein mechanics-and engineering. Combined, single molecule atomic force microscopy and protein engineering efforts are well under way to understand molecular determinants for the mechanical stability of elastomeric proteins and to develop methodologies to tune the mechanical properties of proteins in a rational and systematic fashion, which will lead to the {\textquoteright}mechanical engineering{\textquoteright} of elastomeric proteins. Here the current status of these experimental efforts is discussed and the successes and challenges in constructing novel proteins with tailored nanomechanical proteins are highlighted. The prospect of employing such engineered artificial elastomeric proteins as building blocks for the construction of biomaterials for applications ranging from material sciences to biomedical engineering is also discussed.},
	keywords = {ATOMIC-FORCE MICROSCOPY, BIOLOGICAL ROLES, DIHYDROFOLATE-REDUCTASE, EXTRACELLULAR-MATRIX PROTEIN, FLUORESCENT PROTEIN, IG DOMAIN, MOLECULAR-DYNAMICS SIMULATIONS, PROTEIN, SINGLE, TITIN IMMUNOGLOBULIN DOMAINS, UNFOLDING PATHWAYS},
	isbn = {1616-301X},
	url = {<Go to ISI>://000259933000001},
	author = {Li, H. B.}
}
@article {1350,
	title = {Single molecule force spectroscopy reveals a weakly populated microstate of the FnIII domains of tenascin},
	journal = {Journal of Molecular Biology},
	volume = {361},
	number = {2},
	year = {2006},
	note = {ISI Document Delivery No.: 074WPTimes Cited: 8Cited Reference Count: 48Cao, Y. Li, Hongbin},
	month = {Aug},
	pages = {372-381},
	type = {Article},
	abstract = {The native states of proteins exist as an ensemble of conformationally similar microstates. The fluctuations among different microstates are of great importance for the functions and structural stability of proteins. Here, we demonstrate that single molecule atomic force microscopy (AFM) can be used to directly probe the existence of multiple folded microstates. We used the AFM to repeatedly stretch and relax a recombinant tenascin fragment TNfnALL to allow the fibronectin type III (FnIII) domains to undergo repeated unfolding/refolding cycles. In addition to the native state, we discovered that some FnIII domains can refold from the unfolded state into a previously unrecognized microstate, N* state. This novel state is conformationally similar to the native state, but mechanically less stable. The native state unfolds at similar to 120 pN, while the N* state unfolds at similar to 50 pN. These two distinct populations of microstates constitute the ensemble of the folded states for some FnIII domains. An unfolded FnIII domain can fold into either one of the two microstates via two distinct folding routes. These results reveal the dynamic and heterogeneous picture of the folded ensemble for some FnIII domains of tenascin, which may carry important implications for the mechanical functions of tenascins in vivo. (c) 2006 Elsevier Ltd. All rights reserved.},
	keywords = {DYNAMICS, fluctuations, FnIII domains, HYDROGEN-EXCHANGE, IMMUNOGLOBULIN, MECHANICAL STABILITY, mechanical unfolding, microscopy, MODULES, PROTEIN-STRUCTURE, scanning probe, single-molecule force spectroscopy, tenascin, TITIN, UNFOLDING PATHWAYS},
	isbn = {0022-2836},
	url = {<Go to ISI>://000239842800014},
	author = {Cao, Y. and Li, H. B.}
}
