Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Molecular mechanisms of microheterogeneity-induced defect formation in ferritin crystallization
Autore:
Yau, ST; Thomas, BR; Galkin, O; Gliko, O; Vekilov, PG;
Indirizzi:
Univ Alabama, Dept Chem, Huntsville, AL 35899 USA Univ Alabama HuntsvilleAL USA 35899 Dept Chem, Huntsville, AL 35899 USA Univ Alabama, Ctr Micrograv & Mat Res, Huntsville, AL 35899 USA Univ Alabama Huntsville AL USA 35899 & Mat Res, Huntsville, AL 35899 USA NASA, George C Marshall Space Flight Ctr, Univ Space Res Assoc, Huntsville, AL 35812 USA NASA Huntsville AL USA 35812 iv Space Res Assoc, Huntsville, AL 35812 USA
Titolo Testata:
PROTEINS-STRUCTURE FUNCTION AND GENETICS
fascicolo: 4, volume: 43, anno: 2001,
pagine: 343 - 352
SICI:
0887-3585(20010601)43:4<343:MMOMDF>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
ATOMIC-FORCE MICROSCOPY; EGG-WHITE LYSOZYME; PROTEIN CRYSTALLIZATION; MACROMOLECULAR CRYSTALLIZATION; APOFERRITIN MOLECULES; SURFACE-MORPHOLOGY; GROWTH-KINETICS; CRYSTAL-GROWTH; TAPPING MODE; HUMAN-H;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Vekilov, PG Univ Alabama, Dept Chem, Von Braun Res Hall D-9, Huntsville, AL 35899 USA Univ Alabama Von Braun Res Hall D-9 Huntsville AL USA 35899 SA
Citazione:
S.T. Yau et al., "Molecular mechanisms of microheterogeneity-induced defect formation in ferritin crystallization", PROTEINS, 43(4), 2001, pp. 343-352

Abstract

We apply in situ atomic force microscopy to the crystallization of ferritins from solutions containing approximate to5% (w/w) of their inherent molecular dimers. Molecular resolution imaging shows that the dimers consist of two bound monomers. The constituent monomers are likely partially denatured, resulting in increased hydrophobicity of the dimer surface. Correspondingly, the dimers strongly adsorb on the crystal surface. The adsorbed dimers hinder step growth and on incorporation by the crystal initiate stacks of up to 10 triple and single vacancies in the subsequent crystal layers. The molecules around the vacancies are shifted by approximate to0.1 molecular dimensions from their crystallographic positions. The shifts strain the lattice and, as a consequence, at crystal sizes > 200 mum, the accumulated strain is resolved by a plastic deformation whereupon the crystal breaks into mosaic blocks 20-50 mum in size. The critical size for the onset of mosaicityis similar for ferritin and apoferritin and close to the value for a thirdprotein, lysozyme; it also agrees with theoretical predictions. Trapped microcrystals in ferritin and apoferritin induce strain with a characteristiclength scale equal to that of a single point defect, and, as a consequence, trapping does not contribute to the mosaicity. The sequence of undesired phenomena that include heterogeneity generation, adsorption, incorporation,and the resulting lattice strain and mosaicity in this and other proteins systems, could be avoided by improved methods to separate similar proteins species (microheterogeneity) or by increasing the biochemical stability of the macromolecules against oligomerization. Proteins 2001;43:343-352, (C) 2001 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 14:40:29