@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 {2034,
	title = {Single molecule force spectroscopy reveals engineered metal chelation is a general approach to enhance mechanical stability of proteins},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {105},
	number = {32},
	year = {2008},
	note = {ISI Document Delivery No.: 339EKTimes Cited: 16Cited Reference Count: 44Cao, Yi Yoo, Teri Li, Hongbin},
	month = {Aug},
	pages = {11152-11157},
	type = {Article},
	abstract = {Significant mechanical stability is an essential feature shared by many elastomeric proteins, which function as molecular springs in a wide variety of biological machinery and biomaterials of superb mechanical properties. Despite the progress in understanding molecular determinants of mechanical stability, it remains challenging to rationally enhance the mechanical stability of proteins. Using single molecule force spectroscopy and protein engineering techniques, we demonstrate that engineered bi-histidine metal chelation can enhance the mechanical stability of proteins significantly and reversibly. Based on simple thermodynamic cycle analysis, we engineered a bi-histidine metal chelation site into various locations of the small protein, GB1, to achieve preferential stabilization of the native state over the mechanical unfolding transition state of GB1 through the binding of metal ions. Our results demonstrate that the metal chelation can enhance the mechanical stability of GB1 by as much as 100 pN. Since bi-histidine metal chelation sites can be easily implemented, engineered metal chelation provides a general methodology to enhance the mechanical stability of a wide variety of proteins. This general approach in protein mechanics will enable the rational tuning of the mechanical stability of proteins. It will not only open new avenues toward engineering proteins of tailored nanomechanical properties, but also provide new approaches to systematically map the mechanical unfolding pathway of proteins.},
	keywords = {BINDING SITES, charge, DESIGN, DOMAINS, ELASTICITY, engineering, EXTRACELLULAR-MATRIX PROTEIN, mechanical unfolding, PROTEIN, protein mechanics, rational design, SIMULATIONS, STABILIZATION, STRENGTH, THERMOSTABILITY, TITIN},
	isbn = {0027-8424},
	url = {<Go to ISI>://000258560700024},
	author = {Cao, Y. and Yoo, T. and Li, H. B.}
}
