963 resultados para Triple helix


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Reprinted from Volume 2, chapter 2 of "The Memoirs of Francesco Crispi."

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Available on demand as hard copy or computer file from Cornell University Library.

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Mode of access: Internet.

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"Polarité pathologique ou ce qui a été appelé symétrie dans la maladie, par Burt G. Wilder": p. 132-156.

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Mode of access: Internet.

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"Bibliografía...[de las principales obras del general Mitre]": v.1, p. [383]-390.

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Mimeographed.

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Thesis (Master's)--University of Washington, 2016-06

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The structure of a novel plant defensin isolated from the flowers of Petunia hybrida has been determined by H-1 NMR spectroscopy. P. hybrida defensin 1 (PhD1) is a basic, cysteine-rich, antifungal protein of 47 residues and is the first example of a new subclass of plant defensins with five disulfide bonds whose structure has been determined. PhD1 has the fold of the cysteine-stabilized alphabeta motif, consisting of an alpha-helix and a triple-stranded antiparallel beta-sheet, except that it contains a fifth disulfide bond from the first loop to the alpha-helix. The additional disulfide bond is accommodated in PhD1 without any alteration of its tertiary structure with respect to other plant defensins. Comparison of its structure with those of classic, four-disulfide defensins has allowed us to identify a previously unrecognized hydrogen bond network that is integral to structure stabilization in the family.

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Denote the set of 21 non-isomorphic cubic graphs of order 10 by L. We first determine precisely which L is an element of L occur as the leave of a partial Steiner triple system, thus settling the existence problem for partial Steiner triple systems of order 10 with cubic leaves. Then we settle the embedding problem for partial Steiner triple systems with leaves L is an element of L. This second result is obtained as a corollary of a more general result which gives, for each integer v greater than or equal to 10 and each L is an element of L, necessary and sufficient conditions for the existence of a partial Steiner triple system of order v with leave consisting of the complement of L and v - 10 isolated vertices. (C) 2004 Elsevier B.V. All rights reserved.

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The folding of HIV gp41 into a 6-helix bundle drives virus-cell membrane fusion. To examine the structural relationship between the 6-helix bundle core domain and other regions of gp41, we expressed in Escherichia coli, the entire ectodomain of HIV-2(ST) gp41 as a soluble, trimeric maltose-binding protein (MBP)/gp41 chimera. Limiting proteolysis indicated that the Cys-591-Cys-597 disulfide-bonded region is outside a core domain comprising two peptides, Thr-529-Trp-589 and Val-604-Ser-666. A biochemical examination of MBP/gp41 chimeras encompassing these core peptides; indicated that the N-terminal polar segment, 521-528, and C-terminal membrane-proximal segment, 658-666, cooperate in stabilizing the ectodomain. A functional interaction between sequences outside the gp41 core may contribute energy to membrane fusion. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

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The 2-pyridinecarbaldehyde isonicotinoyl hydrazone (HPCIH) family of ligands are typically tridentate N,N,O chelators that exhibit very high in vitro activity in mobilizing intracellular Fe and are promising candidates for the treatment of Fe overload diseases. Complexation of ferrous perchlorate with HPCIH in MeCN solution gives the expected six-coordinate complex Fe-II(PCIH)(2). However, complexation of Fe-II with 2-pyridinecarbaldehyde picolinoyl hydrazone (HPCPH, an isomer of HPCIH) under the same conditions leads to spontaneous assembly of an unprecedented asymmetric, mixed-ligand dinuclear triple helical complex Fe-2(II)(PCPH)(2)(PPH), where PPH2- is the dianion of bis(picolinoyl) hydrazine. The X-ray crystal structure of this complex shows that each ligand binds simultaneously to both metal centres in a bidentate fashion. The dinuclear complex exhibits two well separated and totally reversible Fe-III/II redox couples as shown by cyclic voltammetry in MeCN solution.