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Titolo:
Structural studies of a crystalline insulin analog complex with protamine by atomic force microscopy
Autore:
Yip, CM; Brader, ML; Frank, BH; DeFelippis, MR; Ward, MD;
Indirizzi:
Eli Lilly & Co, Lilly Res Labs, Indianapolis, IN 46285 USA Eli Lilly & CoIndianapolis IN USA 46285 Labs, Indianapolis, IN 46285 USA Univ Minnesota, Ctr Interfacial Engn, Minneapolis, MN 55455 USA Univ Minnesota Minneapolis MN USA 55455 l Engn, Minneapolis, MN 55455 USA Univ Minnesota, Dept Chem Engn & Mat Sci, Minneapolis, MN 55455 USA Univ Minnesota Minneapolis MN USA 55455 at Sci, Minneapolis, MN 55455 USA
Titolo Testata:
BIOPHYSICAL JOURNAL
fascicolo: 1, volume: 78, anno: 2000,
parte:, 1
pagine: 466 - 473
SICI:
0006-3495(200001)78:1<466:SSOACI>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
TAPPING-MODE; MACROMOLECULAR CRYSTALS; DIRECT VISUALIZATION; MOLECULAR-CRYSTALS; GROWTH; SURFACE; MECHANISMS; PROTEIN; LYS(B28)PRO(B29)-INSULIN; DISSOCIATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Yip, CM Univ Toronto, Inst Biomat & Biomed Engn, 407 Rosebrugh Bldg,4 Taddle CreekRd, Toronto, ON M5S 3G9, Canada Univ Toronto 407 Rosebrugh Bldg,4 Taddle Creek Rd Toronto ON Canada M5S 3G9
Citazione:
C.M. Yip et al., "Structural studies of a crystalline insulin analog complex with protamine by atomic force microscopy", BIOPHYS J, 78(1), 2000, pp. 466-473

Abstract

Crystallographic studies of insulin-protamine complexes, such as neutral protamine Hagedorn (NPH) insulin, have been hampered by high crystal solventcontent, small crystal dimensions, and extensive disorder in the protaminemolecules. We report herein in situ tapping mode atomic force microscopy (TMAFM) studies of crystalline neutral protamine Lys(B28)Pro(B29) (NPL), a complex of Lys(B28)Pro(B29) insulin, in which the C-terminal prolyl and lysyl residues of human insulin are inverted, and protamine that is used as an intermediate time-action therapy for treating insulin-dependent diabetes. Tapping mode AFM performed at 6 degrees C on bipyramidally tipped tetragonalrod-shaped NPL crystals revealed large micron-sized islands separated by 44-Angstrom, tall steps. Lattice images obtained by in situ TMAFM phase and height imaging on these islands were consistent with the arrangement of individual insulin-protamine complexes on the P4(1)2(1)2 (110) crystal plane of NPH, based on a low-resolution x-ray diffraction structure of NPH, arguing that the NPH and NPL insulins are isostructural. Superposition of the height and phase images indicated that tip-sample adhesion was larger in the interstices between NPL complexes in the (110) crystal plane than over the individual complexes. These results demonstrate the utility of low-temperature TMAFM height and phase imaging for the structural characterization of biomolecular complexes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 09:01:30