@article {2673,
	title = {Structures of Water Molecules at the Interfaces of Aqueous Salt Solutions and Silica: Cation Effects},
	journal = {Journal of Physical Chemistry C},
	volume = {113},
	number = {19},
	year = {2009},
	note = {ISI Document Delivery No.: 443FLTimes Cited: 6Cited Reference Count: 53Yang, Zheng Li, Qifeng Chou, Keng C.},
	month = {May},
	pages = {8201-8205},
	type = {Article},
	abstract = {Structures of water molecules at water/silica interfaces, in the presence of alkali chloride. were investigated using infrared-visible sum frequency vibrational spectroscopy. Significant perturbations of the interfacial water structure were observed on silica surfaces with the NaCl concentration as low as 1 x 10(-4) M. The cations, which interact with the Silica Surface via electrostatic interaction, play key roles in Perturbing the hydrogen-bond network of water molecules at the water/silica interface. This cation effect becomes saturated at concentrations around 10(-2) to 10(-1) M, where the sum frequency generation peaks at 3200 and 3400 cm(-1) decrease by 75\%. Different alkali cation species (Li+, Na+, and K+) produce different magnitudes of perturbation, with K+ > Li+ > Na+. This order can be explained by considering the effective ionic radii of the hydrated cations and the electrostatic interactions between the hydrated cations and silica Surfaces. The interfacial water structure associated with the 3200 cm(-1) band is more vulnerable to the cation perturbation, Suggesting that the more ordered water structure on silica is likely associated with the vincinal silanol groups, which create a higher local surface electrical field on silica.},
	keywords = {ADSORPTION, charge, DYNAMICS SIMULATIONS, ELECTROLYTE INTERFACE, hydration, INTERFACE, LIQUID WATER, SOLID/LIQUID, SUM-FREQUENCY SPECTROSCOPY, SURFACE, vibrational spectroscopy},
	isbn = {1932-7447},
	url = {<Go to ISI>://000265895500034},
	author = {Yang, Z. and Li, Q. F. and Chou, K. C.}
}
@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.}
}
