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          Institute: MPI für Biochemie     Collection: Structure Research (R. Huber)     Display Documents

ID: 41647.0, MPI für Biochemie / Structure Research (R. Huber)
Formation of metal nanoclusters on specific surface sites of protein molecules
Authors:Braun, N.; Meining, W.; Hars, U.; Fischer, M.; Ladenstein, R.; Huber, R.; Bacher, A.; Weinkauf, S.; Bachmann, L.
Date of Publication (YYYY-MM-DD):2002-08-09
Title of Journal:Journal of Molecular Biology
Journal Abbrev.:J. Mol. Biol.
Issue / Number:2
Start Page:341
End Page:353
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:During vacuum condensation of metals on frozen proteins, nanoclusters are preferentially formed at specific surface sites (decoration). Understanding the nature of metal/protein interaction is of interest for structure analysis and is also important in the fields of biocompatibility and sensor development. Studies on the interaction between metal and distinct areas on the protein which enhance or impede the probability for cluster formation require information on the structural details of the protein surface underlying the metal clusters. On three enzyme complexes, lumazine synthase from Bacillus subtilis, proteasome from Thermoplasma acidophilum and GTP cyclohydrolase I from Escherichia coli, the decoration sites as determined by electron microscopy (EM) were correlated with their atomic surface structures as obtained by X-ray crystallography. In all three cases, decoration of the same protein results in different cluster distributions for gold and silver. Gold decorates surface areas consisting of polar but uncharged residues and with rough relief whereas silver clusters are preferentially formed on top of protein pores outlined by charged and hydrophilic residues and filled with frozen buffer under the experimental conditions. A common quality of both metals is that they strictly avoid condensation on hydrophobic sites lacking polar and charged residues. The results open ways to analyse the binding mechanism of nanoclusters to small specific sites on the surface of hydrated biomacro-molecules by non-microscopic, physical-chemical methods. Understanding the mechanism may lead to advanced decoration techniques resulting in fewer background clusters. This would improve the analysis of single molecules with regard to their symmetries and their orientation in the adsorbed state and in precrystalline assemblies as well as facilitate the detection of point defects in crystals caused by misorientation or by impurities. (C) 2002 Elsevier Science Ltd. All rights reserved.
Free Keywords:nanoclusters; decoration; metal/protein interaction; electron microscopy; protein crystallization
Comment of the Author/Creator:Date: 2002, AUG 9
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Structure Research (Huber)
External Affiliations:Tech Univ Munich, Dept Chem, Lichtenbergstr 4, D-85748; Garching, Germany; Tech Univ Munich, Dept Chem, D-85748 Garching, Germany; Karolinska Inst, Novum, Ctr Struct Biochem, S-14157 Huddinge, Sweden; Innsbruck Univ, Inst Chem Phys, A-6020 Innsbruck, Austria
Identifiers:ISI:000177488000014 [ID No:1]
ISSN:0022-2836 [ID No:2]
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