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Titolo: LUMBRICUSTERRESTRIS HEMOGLOBIN  A COMPARISON OF SMALLANGLE XRAYSCATTERING AND CRYOELECTRON MICROSCOPY DATA
Autore: KREBS A; LAMY J; VINOGRADOV SN; ZIPPER P;
 Indirizzi:
 KARL FRANZENS UNIV GRAZ,INST PHYS CHEM,HEINRICHSTR 28 A8010 GRAZ AUSTRIA KARL FRANZENS UNIV GRAZ,INST PHYS CHEM A8010 GRAZ AUSTRIA UNIV TOURS,GRP ANAL STRUCT ANTIGENES F37032 TOURS FRANCE WAYNE STATE UNIV,DEPT BIOCHEM DETROIT MI 48201
 Titolo Testata:
 Biopolymers
fascicolo: 4,
volume: 45,
anno: 1998,
pagine: 289  298
 SICI:
 00063525(1998)45:4<289:LHACO>2.0.ZU;2G
 Fonte:
 ISI
 Lingua:
 ENG
 Soggetto:
 GIANT EXTRACELLULAR HEMOGLOBIN; QUATERNARY STRUCTURE; DODECAMER SUBUNIT; 3DIMENSIONAL RECONSTRUCTION; MACROBDELLADECORA; GLOBIN COMPLEXES; DISSOCIATION; EARTHWORM; CHAINS; SHAPE;
 Keywords:
 HEMOGLOBIN; HEXAGONAL BILAYER; LUMBRICUS; ELECTRON MICROSCOPY; 3DIMENSIONAL RECONSTRUCTION; SMALLANGLE XRAY SCATTERING; 3DIMENSIONAL MODELS;
 Tipo documento:
 Article
 Natura:
 Periodico
 Settore Disciplinare:
 Science Citation Index Expanded
 Science Citation Index Expanded
 Citazioni:
 25
 Recensione:
 Indirizzi per estratti:



 Citazione:
 A. Krebs et al., "LUMBRICUSTERRESTRIS HEMOGLOBIN  A COMPARISON OF SMALLANGLE XRAYSCATTERING AND CRYOELECTRON MICROSCOPY DATA", Biopolymers, 45(4), 1998, pp. 289298
Abstract
The quaternary structure of Lumbricus terrestris hemoglobin was investigated by smallangle xray scattering (SAXS). Based on the SAXS datafrom several independent experiments, a threedimensional (30) consensus model was established to simulate the solution structure of this complex protein at low resolution (about 3 nm) and to yield the particle dimensions. The model is built up from ct large number of small spheres of different weights, a result of the twostep procedure used to calculate the SAXS model. It accounts for the arrangement of 12 subunits in a hexagonal bila),er structure and for an additional central unitof cylinderlike shape. This model provides an excellent fit of the experimental scattering curve of the protein up to h = 1 nm(1) and a nearly perfect fit of the experimental distance distribution function p(r) in the whole range. Scattering curves and p(r)functions were also calculated for lowresolution models based on 30 reconstructions obtained by cryoelectron microscopy (EM). The calculated functions of thesemodels also provide a very good fit of the experimental scattering curve (even at h > I nm(1)) and p(r) function, if hydration is taken into account and the original model coordinates are slightly rescaled. The comparison of models reveals that both the SAXSbased and the EMbased model lend to a similar simulation of the protein structure and tosimilar particle dimensions. The essential differences between the models concern the hexagonal bilayer arrangement (eclipsed in the SAXS model, one layer slightly rotated in the EM model), and the mass distribution, mainly oil the surface and in the central part of the protein complex. (C) 1998 John Wiley & Sons, Inc.
ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 06:13:43