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Small Molecule Analogs of Phospholipid-Metal Ion Binding Sites: Synthesis and Molecular Modeling of Cyclohexane-1,2,4-triol Trisphosphates

Autor: S.W. Shuey, Lee G. Pedersen, R. G. Hiskey, J. C. Amburgey

Publikováno v: Bioorganic Chemistry. 22:172-197

Four diastereomeric cyclohexane-1,2,4-triol trisphosphates were synthesized to serve as small molecule analogs of putative phospholipid-metal ion binding sites. The parent cyclehexane-1,2,4-triols were prepared and phosphorylated. Deprotection of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::343c0e1f8625a4d0957ad820b60a43a9
https://doi.org/10.1006/bioo.1994.1014

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Small Molecule Analogs of Phospholipid Metal-Ion Binding Sites: Potentiometric and Spectroscopic Studies of Mg(II) and Ca(II) Complexes of Cyclohexane-1,2,4-Triol Trisphosphates

Autor: Nam-Won Huh, Lee G. Pedersen, R. G. Hiskey, J. C. Amburgey

Publikováno v: Bioorganic Chemistry. 22:198-215

Studies on the Mg(II) and Ca(II) complexes of four diastereomeric cyclohexane-1,2,4-triol trisphosphates were conducted using 1H NMR, 31P NMR, and calcium ion selective electrode (ISE) titrations. Based on the trends in Mg(II) and Ca(II) ion affinity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::34edf76d370b8994bc6d00db59d124e6
https://doi.org/10.1006/bioo.1994.1015

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A metal ion-binding site in the kringle region of bovine prothrombin fragment 1

Autor: P, Berkowitz, N W, Huh, K E, Brostrom, M G, Panek, D J, Weber, A, Tulinsky, L G, Pedersen, R G, Hiskey

Publikováno v: The Journal of biological chemistry. 267(7)

45Ca(II) binding studies (equilibrium dialysis) on the kringle domain of bovine prothrombin fragment 1 were conducted using a mixture of peptides (residues 43-156 and 46-156) resulting from limited alpha-chymotryptic hydrolysis of fragment 1. Analysi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4bf8098db0eb4c09b4995ede0d1afaa0
https://pubmed.ncbi.nlm.nih.gov/1311313

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The nature of the slow metal ion-dependent conformational transition in bovine prothrombin

Autor: K A Koehler, H C Marsh, R G Hiskey, M E Scott

Publikováno v: Biochemical Journal. 183:513-517

Kinetic parameters characterizing the slow structural isomerization observed via metal ion-dependent intrinsic fluorescence quenching of bovine prothrombin Fragment 1 have been determined. From forward and reverse rate constants, an equilibrium const

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e1f6517429f6e68da45fd8b0078dece
https://doi.org/10.1042/bj1830513

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Conformation and structure of a blocked Gla residue: N-benzyloxycarbonyl-(γ,γ-di-tert-butyl)-L-carboxyglutamic acid α-methyl ester

Autor: R. G. Hiskey, Derek J. Hodgson, D. W. Deerfield, Y. Yokomori

Publikováno v: Acta Crystallographica Section C Crystal Structure Communications. 43:1567-1569

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4cdb98186ed86c7b53a83511d2d40844
https://doi.org/10.1107/s0108270187091066

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A kinetic model describing the interaction of bovine prothrombin fragment 1 with calcium ions

Autor: C W, Kabis, M M, Sarasua, K E, Gottschalk, C D, Bourne, L G, Pedersen, C M, Jackson, R G, Hiskey, K A, Koehler

Publikováno v: Thrombosis and haemostasis. 53(1)

A kinetic model is derived for the interaction of bovine prothrombin fragment 1 with calcium ions. The model requires binding of a minimum of two calcium ions for induction of the observed biphasic fluorescence decrease as a function of time. The mod

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e867e6f7bea5a8c6161f3a6c85b70910
https://pubmed.ncbi.nlm.nih.gov/3838826

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