@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.}
}
