@article {678,
	title = {Template effect where 1-3 molecules drive formation of a trimer carceplex},
	journal = {Chemistry-a European Journal},
	volume = {9},
	number = {14},
	year = {2003},
	note = {ISI Document Delivery No.: 706XATimes Cited: 6Cited Reference Count: 46},
	month = {Jul},
	pages = {3253-3262},
	type = {Article},
	abstract = {The template effect in the formation of a trimer carceplex using 1-3 molecules as templates is explored. Thirteen different templates were studied and template ratios were measured for templates of like and unlike molecularity. Five transition-state models were studied for their binding abilities to see if these mirror the template ratios. The chemical shifts of the guests and the thermodynamic and kinetic values for templation suggest that binding is key, often tight, and that the guest determining step is formation of the last covalent bond. The molecular dynamics of guests as well as the conformational dynamics of both hosts and guests further addresses nature of the recognition between host and guest. Finally, we were surprised to discover that water can bind reversibly to the trimer carceplexes, which will have ramifications to any inner phase reactions conducted inside the cage.},
	keywords = {AMPLIFICATION, BARRIER, BINDING, CAPTURE, carceplex, CHEMISTRY, DIELS-ALDER REACTION, DYNAMICS, ELUCIDATION, ENCAPSULATION, HOST-GUEST COMPLEXATION, host-guest systems, molecular recognition, RESORCINARENE CAPSULE, REVERSIBLE, supramolecular, TEMPLATE SYNTHESIS},
	isbn = {0947-6539},
	url = {<Go to ISI>://000184479300009},
	author = {Makeiff, D. A. and Sherman, J. C.}
}
@article {4312,
	title = {Equus caballus gelsolin - cDNA sequence and protein structural implications},
	journal = {European Journal of Biochemistry},
	volume = {251},
	number = {3},
	year = {1998},
	note = {ISI Document Delivery No.: YV719Times Cited: 4Cited Reference Count: 48},
	month = {Feb},
	pages = {613-621},
	type = {Article},
	abstract = {We have generated and characterized the cDNA from equine smooth muscle that Encodes gelsolin, an actin-modulating protein. Overlapping cDNA clones synthesized by the reverse transcriptaseoplymerase chain reaction and clones isolated from a horse genomic library provided the complete primary structure for the intracellular isoform of gelsolin, while cDNA complemented with protein sequence data produced the full-length primary transcript of the gelsolin isoform found circulating in equine plasma. The deduced amino acid sequences of the intracellular and secreted versions of equine gelsolin infer polypeptides of 731 and 755 residues with apparent molecular masses of 80.7 kDa and 83.2 kDa, respectively. Multiple sequence alignment analysis of equine, human, porcine, and murine orthologs of gelsolin demonstrates prominent similarities among all of these proteins, with the horse and human molecules exhibiting the largest degree of likeness with respect to polypeptide length and overall sequence composition. Both horse and human plasma gelsolins are comprised of 755 amino acids with 94\% of the residues identical, while the degree of sequence identity in the shorter (731 residues) cytoplasmic gelsolins is 95 \%. Analysis of the sequences and structures of the six related domains that comprise gelsolin emphasizes the strong correlation that exists between primary structural conservation among mammalian gelsolins and maintenance of the three-dimensional domain fold characteristic of members of this protein family.},
	keywords = {actin-binding protein, ACTIN-SEVERING PROTEINS, amino acid sequence, AMPLIFICATION, BINDING DOMAIN, cDNA sequence, CLONING, CYTOPLASMIC FORMS, DNA, END, extraction, gelsolin, HORSE PLASMA GELSOLIN, MUSCLE, protein structure},
	isbn = {0014-2956},
	url = {<Go to ISI>://000071855900009},
	author = {Koepf, E. K. and Hewitt, J. and Vo, H. and MacGillivray, R. T. A. and Burtnick, L. D.}
}
