@article {1545,
	title = {Characterization of de novo four-helix bundles by molecular dynamics simulations},
	journal = {Proteins-Structure Function and Bioinformatics},
	volume = {64},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 064QITimes Cited: 5Cited Reference Count: 34Scott, Walter R. P. Seo, Emily Huttunen, Heidi Wallhorn, Diana Sherman, John C. Straus, Suzana K.},
	month = {Aug},
	pages = {719-729},
	type = {Article},
	abstract = {We have investigated the structure and dynamics of three cavitand-based four-helix bundles (caviteins) by computer simulation. In these systems, designed de novo, each of the four helices contain the identical basis sequence EELLKKLEELLKKG (N1). Each cavitein consists of a rigid macrocycle (cavitand) with four aryl linkages, to each of which is connected an NI peptide by means of a linker peptide. The three caviteins studied here differ only in the linker peptide, which consist of one, two, or three glycine residues. Previous experimental work has shown that these systems exhibit very different behavior in terms of stability and oligomerization states despite the small differences in the linker peptide. Given that to date no three-dimensional structure is available for these caviteins, we have undertaken a series of molecular dynamics (MD) simulations in explicit water to try to rationalize the large differences in the experimentally observed behavior of these systems. Our results provide insight, for the first time, into why and how the cavitein with a single glycine linker forms dimers. In addition, our results indicate why although the two- and three-glycine-linked caviteins have similar stabilities, they have different native-like characteristics: the cavitein with three glycines can form a supercoiled helix, whereas the one with two glycines cannot. These findings may provide a useful guide in the rational de novo design of novel proteins with finely tunable structures and functions in the future.},
	keywords = {caviteins, de novo four-helix bundle, DESIGN, DOMAIN, HELICAL BUNDLES, molecular dynamics simulations, PEPTIDE, PROTEIN DESIGN, PROTEINS, STATE, SYSTEM, TASP, template-assembled synthetic protein},
	isbn = {0887-3585},
	url = {<Go to ISI>://000239103800014},
	author = {Scott, W. R. P. and Seo, E. and Huttunen, H. and Wallhorn, D. and Sherman, J. C. and Straus, S. K.}
}
@inbook {980,
	title = {Cavitand based four-helix bundles},
	booktitle = {Peptide Revolution: Genomics, Proteomics \& Therapeutics},
	year = {2004},
	note = {ISI Document Delivery No.: BEQ46Times Cited: 0Cited Reference Count: 8Seo, Emily S. Sherman, John C.Proceedings Paper18th American Peptide SymposiumJUL 19-23, 2003BOSTON, MA1155 SIXTEENTH ST NW, WASHINGTON, DC 20036 USA},
	pages = {246-247},
	publisher = {Amer Chemical Soc},
	organization = {Amer Chemical Soc},
	address = {Washington},
	keywords = {PROTEIN DESIGN, TASP},
	isbn = {0-9715560-1-6},
	url = {<Go to ISI>://000238911100106},
	author = {Seo, E. S. and Sherman, J. C.},
	editor = {Chorev, M. and Sawyer, T. K.}
}
@inbook {889,
	title = {De novo four-helix bundle proteins},
	booktitle = {Peptide Revolution: Genomics, Proteomics \& Therapeutics},
	year = {2004},
	note = {ISI Document Delivery No.: BEQ46Times Cited: 0Cited Reference Count: 7Huttunen, Heidi K. Sherman, John C.Proceedings Paper18th American Peptide SymposiumJUL 19-23, 2003BOSTON, MA1155 SIXTEENTH ST NW, WASHINGTON, DC 20036 USA},
	pages = {244-245},
	publisher = {Amer Chemical Soc},
	organization = {Amer Chemical Soc},
	address = {Washington},
	keywords = {CAVITANDS, TASP},
	isbn = {0-9715560-1-6},
	url = {<Go to ISI>://000238911100105},
	author = {Huttunen, H. K. and Sherman, J. C.},
	editor = {Chorev, M. and Sawyer, T. K.}
}
@article {342,
	title = {A comparison of three- and four-helix bundle TASP molecules},
	journal = {Journal of Peptide Science},
	volume = {8},
	number = {6},
	year = {2002},
	note = {ISI Document Delivery No.: 563ZTTimes Cited: 14Cited Reference Count: 19},
	month = {Jun},
	pages = {275-282},
	type = {Article},
	abstract = {We have designed, synthesized and characterized three- and four-helix bundle template-assembled synthetic proteins (TASPs). The TASPs were synthesized using disulphide bonds between the peptides and either the cyclotribenzylene (CTB) template, or the cavitand (BOWL) template, to form the three- and four helix bundles, respectively. The TASPs were constructed using peptides that were linked via their N-termini (peptide CGGGEELLKKXEELLKKG, where X = L, I, Nle or V), or via their C-termini (peptide GEELLKKLEELLKKGGGC). Each TASP was assayed for its structure, stability, {\textquoteright}native-like{\textquoteright} characteristics and whether it was a monomer in solution. All TASPs were found to be highly helical, and highly resistant to chemical denaturation using guanidine hydrochloride (GnHCl). Analysis of the GnHCl-induced unfolding curves of the different TASPs demonstrated stability differences based on the number of helices in the bundle, the end of the helix that was attached to the template, and the identity of the core amino acid. The TASPs all had molten-globule structure, which is (generally) consistent with a degenerate sequence in the core. The four-helix bundle TASPs appeared to be monomers in solution, whereas there is some evidence that the three-helix bundle TASPs are weakly self associating. Copyright. (C) 2002 European Peptide Society and John Wiley Sons, Ltd.},
	keywords = {4-HELIX BUNDLES, DESIGN, four-helix bundle, PROTEIN, STABILITY, TASP, template assembled synthetic protein, three-helix bundle},
	isbn = {1075-2617},
	url = {<Go to ISI>://000176289000005},
	author = {Causton, A. S. and Sherman, J. C.}
}
@article {4500,
	title = {Design of proteins using rigid organic macrocycles as scaffolds},
	journal = {Bioorganic \& Medicinal Chemistry},
	volume = {7},
	number = {1},
	year = {1999},
	note = {ISI Document Delivery No.: 173QETimes Cited: 21Cited Reference Count: 39},
	month = {Jan},
	pages = {23-27},
	type = {Article},
	abstract = {We have designed and synthesized new three-helix template-assembled synthetic proteins (TASPs) 1a-c. The template was the rigid cyclotribenzylene (CTB) macrocycle 2, which has C-3 symmetry. Thiol moieties on the CTB template were used to link cysteine-containing peptide strands 3a-c via disulfide bonds. With designed peptide strands of 15 and 18 residues in length, the structure of TASPs 1a-c were determined to be helical in water according to circular dichroism (CD) spectroscopy. The helicities of TASPs la-e were unchanged over large ranges of pH (2-12) and salt concentrations (0-2 M KCl). TASPs 1a-c were also extremely resistant to chemical denaturants: it requires a guanidine hydrochloride (GnHCl) concentration of 7.4 M for TASPs 1a-c to lose 50\% of their helicity. The major force for stabilization of TASPs 1a-c is the hydrophobic bundling of the helices. (C) 1999 Elsevier Science Ltd. All rights reserved.},
	keywords = {4-HELIX BUNDLE PROTEIN, ASSEMBLED SYNTHETIC PROTEINS, CHEMOSELECTIVE LIGATION, CONSTRUCTION, CROSS-LINKING, CRYSTAL-STRUCTURE, cyclotribenzylene, de novo protein, DE-NOVO PROTEINS, HELICAL BUNDLES, HELICAL PROTEIN, PEPTIDE, TASP, TEMPLATE},
	isbn = {0968-0896},
	url = {<Go to ISI>://000078990600004},
	author = {Causton, A. S. and Sherman, J. C.}
}
@article {3342,
	title = {EFFICIENT COUPLING OF AMINO-ACID DERIVATIVES TO RIGID ORGANIC SCAFFOLDS - MODEL SYNTHESES FOR DE-NOVO PROTEINS},
	journal = {Tetrahedron},
	volume = {51},
	number = {32},
	year = {1995},
	note = {ISI Document Delivery No.: RM784Times Cited: 34Cited Reference Count: 42},
	month = {Aug},
	pages = {8719-8732},
	type = {Article},
	abstract = {We describe the coupling of amino acid derivatives to four different rigid organic macrocycles. The couplings were achieved in high yields, which augurs well for the coupling of polypeptides to the rigid macrocycles to create a new family of de novo proteins. We discuss the structure of the model compounds based on the hydrogen bonding patterns that are evident from their NMR and IR spectra.},
	keywords = {BUNDLE PROTEIN, DESIGN, PEPTIDE, TASP},
	isbn = {0040-4020},
	url = {<Go to ISI>://A1995RM78400004},
	author = {Gibb, B. C. and Mezo, A. R. and Causton, A. S. and Fraser, J. R. and Tsai, F. C. S. and Sherman, J. C.}
}
@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.}
}
