@article {2415,
	title = {X-ray Crystal Analysis of a TASP: Structural Insights of a Cavitein Dimer},
	journal = {Journal of the American Chemical Society},
	volume = {131},
	number = {21},
	year = {2009},
	note = {ISI Document Delivery No.: 451QOTimes Cited: 0Cited Reference Count: 75Freeman, Jon O. Lee, Woo Cheol Murphy, Michael E. P. Sherman, John C.},
	month = {Jun},
	pages = {7421-7429},
	type = {Article},
	abstract = {Cavitein Q4 is a template assembled synthetic protein designed for X-ray crystallographic analysis. It is based on a previous monomeric helical bundle cavitein (N1GG) that consists of four identical parallel helical peptides. Crystals that were grown in the presence of bromide ions were used to solve the initial phases via single-wavelength anomalous dispersion (SAD). A 1.4 angstrom resolution data set was then refined starting with the SAD phases to provide the crystal structure of cavitein Q4. The crystal structure revealed cavitein Q4 as an asymmetric dimer, although the cavitein appears to be largely monomeric in solution. A comparative analysis is carried out to discern any intrinsic differences between Q4 and its parent cavitein N1GG. We present herein the first X-ray crystal structure of a TASP system and relate this structure to the solution data for both Q4 and its parent N1GG.},
	keywords = {4-HELIX BUNDLE, ALPHA-HELICES, ANALYTICAL, ANION-BINDING, ASSEMBLED SYNTHETIC PROTEINS, DE-NOVO PROTEINS, NATIVE-LIKE STRUCTURE, PEPTIDE-CAVITANDS, PROTEINS, SELF-ASSOCIATION, ULTRACENTRIFUGATION, UPPER RIM},
	isbn = {0002-7863},
	url = {<Go to ISI>://000266484900042},
	author = {Freeman, J. O. and Lee, W. C. and Murphy, M. E. P. and Sherman, J. C.}
}
@article {4617,
	title = {Cavitands are effective templates for inducing stability and nativelike structure in de Novo four-helix bundles},
	journal = {Journal of the American Chemical Society},
	volume = {121},
	number = {39},
	year = {1999},
	note = {ISI Document Delivery No.: 243QXTimes Cited: 40Cited Reference Count: 92},
	month = {Oct},
	pages = {8983-8994},
	type = {Article},
	abstract = {We have designed, synthesized and characterized eight cavitand-based de novo four-helix bundles, where each helix contains the basis sequence EELLKKLEELLKKG. We find that each de novo protein is highly helical and extremely stable to the chemical denaturant guanidine hydrochloride (GuHCl). We studied the effect of the cavitand-peptide linker on the stability of each de novo protein. Flexible linkers render the helical structures more susceptible to denaturation by GuHCl. Linker structure and length also dictate monomer/dimer equilibria of the proteins. Proteins containing 0-3 Cry units possess varying degrees of nativelike structure. In contrast, proteins containing two or four methylene Linkers are more characteristic of molten globules. These differences can be attributed to the additional hydrogen bonding capabilities of the glycine linker variants and to the distance between the cavitand template and the helical bundle. The cavitand pendent group was also changed in one de novo protein from a methyl group to a propyl-phosphate moiety. This alteration does not affect the stability or packing within the helical bundle; however, it does affect the monomer/dimer equilibrium.},
	keywords = {4-HELIX BUNDLE, ASSEMBLED, conformational, DESIGNED PROTEIN, HOST GUEST COMPLEXATION, HYDROGEN-EXCHANGE, MOLTEN GLOBULE, NONPOLAR AMINO-ACIDS, rational design, STABILITY, SYNTHETIC PROTEINS, ULTRAVIOLET CIRCULAR-DICHROISM},
	isbn = {0002-7863},
	url = {<Go to ISI>://000083009700003},
	author = {Mezo, A. R. and Sherman, J. C.}
}
