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Titolo:
LUMBRICUS-TERRESTRIS HEMOGLOBIN - A COMPARISON OF SMALL-ANGLE X-RAY-SCATTERING AND CRYOELECTRON MICROSCOPY DATA
Autore:
KREBS A; LAMY J; VINOGRADOV SN; ZIPPER P;
Indirizzi:
KARL FRANZENS UNIV GRAZ,INST PHYS CHEM,HEINRICHSTR 28 A-8010 GRAZ AUSTRIA KARL FRANZENS UNIV GRAZ,INST PHYS CHEM A-8010 GRAZ AUSTRIA UNIV TOURS,GRP ANAL STRUCT ANTIGENES F-37032 TOURS FRANCE WAYNE STATE UNIV,DEPT BIOCHEM DETROIT MI 48201
Titolo Testata:
Biopolymers
fascicolo: 4, volume: 45, anno: 1998,
pagine: 289 - 298
SICI:
0006-3525(1998)45:4<289:LH-ACO>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
GIANT EXTRACELLULAR HEMOGLOBIN; QUATERNARY STRUCTURE; DODECAMER SUBUNIT; 3-DIMENSIONAL RECONSTRUCTION; MACROBDELLA-DECORA; GLOBIN COMPLEXES; DISSOCIATION; EARTHWORM; CHAINS; SHAPE;
Keywords:
HEMOGLOBIN; HEXAGONAL BILAYER; LUMBRICUS; ELECTRON MICROSCOPY; 3-DIMENSIONAL RECONSTRUCTION; SMALL-ANGLE X-RAY SCATTERING; 3-DIMENSIONAL 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., "LUMBRICUS-TERRESTRIS HEMOGLOBIN - A COMPARISON OF SMALL-ANGLE X-RAY-SCATTERING AND CRYOELECTRON MICROSCOPY DATA", Biopolymers, 45(4), 1998, pp. 289-298

Abstract

The quaternary structure of Lumbricus terrestris hemoglobin was investigated by small-angle x-ray scattering (SAXS). Based on the SAXS datafrom several independent experiments, a three-dimensional (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 two-step 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 cylinder-like 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 low-resolution 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 SAXS-based and the EM-based 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.

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Documento generato il 25/11/20 alle ore 06:13:43