@article {2035,
	title = {Protein-protein interaction regulates proteins{\textquoteright} mechanical stability},
	journal = {Journal of Molecular Biology},
	volume = {378},
	number = {5},
	year = {2008},
	note = {ISI Document Delivery No.: 305IOTimes Cited: 10Cited Reference Count: 38Cao, Yi Yoo, Teri Zhuang, Shulin Li, Hongbin},
	month = {May},
	pages = {1132-1141},
	type = {Article},
	abstract = {Elastomeric proteins are molecular springs found not only in a variety of biological machines and tissues, but also in biomaterials of superb mechanical properties. Regulating the mechanical stability of elastomeric proteins is not only important for a range of biological processes, but also critical for the use of engineered elastomeric proteins as building blocks to construct nanomechanical devices and novel materials of well-defined mechanical properties. Here we demonstrate that protein-protein interactions can potentially serve as an effective means to regulate the mechanical properties of elastomeric proteins. We show that the binding of fragments of IgG antibody to a small protein, GB1, can significantly enhance the mechanical stability of GB1. The regulation of the mechanical stability of GB1 by IgG fragments is not through direct modification of the interactions in the mechanically key region of GB1; instead, it is accomplished via the long-range coupling between the IgG binding site and the mechanically key region of GB1. Although Fc and Fab bind GB1 at different regions of GB1, their binding to GB1 can increase the mechanical stability of GB1 significantly. Using alanine point mutants of GB1, we show that the amplitude of mechanical stability enhancement of GB1 by Fc does not correlate with the binding affinity, suggesting that binding affinity only affects the population of GB1/human Fc (hFc) complex at a given concentration of hFc, but does not affect the intrinsic mechanical stability of the GB1/hFc complex. Furthermore, our results indicate that the mechanical stability enhancement by IgG fragments is robust and can tolerate sequence/structural perturbation to GB1. Our results demonstrate that the protein-protein interaction is an efficient approach to regulate the mechanical stability of GB1-like proteins and we anticipate that this new methodology will help to develop novel elastomeric proteins with tunable mechanical stability and compliance. (C) 2008 Elsevier Ltd. All rights reserved.},
	keywords = {BINDING, BIOLOGICAL ROLES, CRYSTAL-STRUCTURE, DIHYDROFOLATE-REDUCTASE, DOMAIN, ENGINEERING PROTEINS, FORCE SPECTROSCOPY, FRAGMENT, HUMAN-IGG, MECHANICAL STABILITY, mechanical unfolding, MOLECULAR ELASTICITY, protein-protein interaction, single molecule atomic force microscopy, STABILIZATION},
	isbn = {0022-2836},
	url = {<Go to ISI>://000256171900015},
	author = {Cao, Y. and Yoo, T. and Zhuang, S. L. and Li, H. B.}
}
@article {1289,
	title = {Arylfluoroborates and alkylfluorosilicates as potential PET imaging agents: High-yielding aqueous biomolecular F-18-labeling},
	journal = {Journal of the American Chemical Society},
	volume = {127},
	number = {38},
	year = {2005},
	note = {ISI Document Delivery No.: 968OCTimes Cited: 29Cited Reference Count: 32},
	month = {Sep},
	pages = {13094-13095},
	type = {Article},
	keywords = {AVIDIN, biotin, BORONIC ACIDS, CROSS-COUPLING REACTIONS, F-18, FRAGMENT, MICROPET, MONOCLONAL-ANTIBODY, PROTEIN, STATE},
	isbn = {0002-7863},
	url = {<Go to ISI>://000232170800007},
	author = {Ting, R. and Adam,Michael J. and Ruth, T. J. and Perrin,David M.}
}
@article {1289,
	title = {Arylfluoroborates and alkylfluorosilicates as potential PET imaging agents: High-yielding aqueous biomolecular F-18-labeling},
	journal = {Journal of the American Chemical Society},
	volume = {127},
	number = {38},
	year = {2005},
	note = {ISI Document Delivery No.: 968OCTimes Cited: 29Cited Reference Count: 32},
	month = {Sep},
	pages = {13094-13095},
	type = {Article},
	keywords = {AVIDIN, biotin, BORONIC ACIDS, CROSS-COUPLING REACTIONS, F-18, FRAGMENT, MICROPET, MONOCLONAL-ANTIBODY, PROTEIN, STATE},
	isbn = {0002-7863},
	url = {<Go to ISI>://000232170800007},
	author = {Ting, R. and Adam,Michael J. and Ruth, T. J. and Perrin,David M.}
}
@article {395,
	title = {(eta(5)-cyclopentadienyl)(p-fluorophenoxo)(nitrosyl)(trimethylsilyl- methyl)molybdenum(II)},
	journal = {Acta Crystallographica Section C-Crystal Structure Communications},
	volume = {58},
	year = {2002},
	note = {ISI Document Delivery No.: 520RZTimes Cited: 1Cited Reference Count: 11Part 2},
	month = {Feb},
	pages = {m68-m69},
	type = {Article},
	abstract = {The title complex, [Mo(C5H5)(C6H4FO)(C4H11Si)(NO)], is formed by reacting CpMo(NO)(CH2SiMe3)(2), where Cp is cyclopentadienyl, with one equivalent of p-FC6H4OH. The complex exhibits the expected piano-stool molecular structure, with a linear nitrosyl ligand [Mo-N-O 168.2 (2)degrees] having Mo-N and N-O distances of 1.764 (2) and 1.207 (3) Angstrom, respectively. The phenoxo Mo-O distance of 1.945 (2) Angstrom is suggestive of some multiple-bond character.},
	keywords = {BONDS, COMPLEXES, FRAGMENT, REACTIVITY},
	isbn = {0108-2701},
	url = {<Go to ISI>://000173796300004},
	author = {Hayton, T. W. and Legzdins,Peter and Rettig, S. J.}
}
@article {466,
	title = {Unusual thermal C-H bond activation by a tungsten allene complex},
	journal = {Journal of the American Chemical Society},
	volume = {124},
	number = {32},
	year = {2002},
	note = {ISI Document Delivery No.: 582NTTimes Cited: 8Cited Reference Count: 18},
	month = {Aug},
	pages = {9380-9381},
	type = {Article},
	keywords = {ALKANES, FRAGMENT, LIGAND},
	isbn = {0002-7863},
	url = {<Go to ISI>://000177358600029},
	author = {Ng, S. H. K. and Adams, C. S. and Legzdins,Peter}
}
@article {3550,
	title = {ADHESION OF MAMMALIAN-CELLS TO A RECOMBINANT ATTACHMENT FACTOR, CBD/RGD, ANALYZED BY IMAGE-ANALYSIS},
	journal = {Biotechnology and Bioengineering},
	volume = {46},
	number = {3},
	year = {1995},
	note = {ISI Document Delivery No.: QR821Times Cited: 16Cited Reference Count: 26},
	month = {May},
	pages = {185-193},
	type = {Article},
	abstract = {A luminance thresholding procedure was developed to quantify cell attachment of a variety of cell lines to CBD/RGD, a hybrid attachment factor comprising a cellulose binding domain and the fibronectin-like RGD attachment peptide. The technique used local thresholding, median filtering, and opening to separate and count cells on each image. Cell lines exhibited three different patterns of attachment to CBD/RGD, depending on whether it was immobilized on polystyrene or cellulose acetate. Vero, COS, HFF, 3T3, 293, and U373 cells attached well to CBD/RGD immobilized on polystyrene or cellulose acetate. CHO, MRC-5, and HEp-2 cells attached to CBD/RGD immobilized on polystyrene, but not to CBD/RGD immobilized on cellulose acetate. BHK and L cells failed to attach to CBD/RGD immobilized on either polystyrene or cellulose acetate. The attachment of many cell lines to CBD/RGD was comparable with attachment of these cells to fibronectin. (C) 1995 John Wiley \& Sons, Inc.},
	keywords = {ALPHA-V, ARG-GLY-ASP, CELL ATTACHMENT, CELLULASE, CELLULOMONAS FIMI, FIBRONECTIN, FRAGMENT, GROWTH, HEPARIN-BINDING, IMAGE ANALYSIS, MAMMALIAN CELLS, RECEPTOR, RECOGNITION SIGNAL, SURFACES, VITRONECTIN},
	isbn = {0006-3592},
	url = {<Go to ISI>://A1995QR82100001},
	author = {Wierzba, A. and Reichl, U. and Turner, R. F. B. and Warren, R. A. J. and Kilburn, D. G.}
}
