MersV1, PubMed, Corpus, bibRecord, 002260

Immobilization and AFM of single 4 x 6-mer tarantula hemocyanin molecules.

Identifieur interne : 002260 ( PubMed/Corpus ); précédent : 002259; suivant : 002261

Immobilization and AFM of single 4 x 6-mer tarantula hemocyanin molecules.

Auteurs : Wolfgang Erker ; Volker Scheumann ; Marco Möller ; Wolfgang Knoll ; Jürgen Rühe ; Heinz Decker

Source :

Micron (Oxford, England : 1993) [ 0968-4328 ] ; 2006.

RBID : pubmed:16632369

English descriptors

KwdEn :
- Air, Aluminum Silicates, Animals, Glass, Gold, Hemocyanins (isolation & purification), Hemocyanins (ultrastructure), Image Enhancement (methods), Microscopy, Atomic Force, Preservation, Biological (methods), Spiders (chemistry), Succinimides.
MESH :
- chemical , isolation & purification : Hemocyanins.
- chemical , ultrastructure : Hemocyanins.
- chemical : Aluminum Silicates, Gold, Succinimides.
- chemistry : Spiders.
- methods : Image Enhancement, Preservation, Biological.
- Air, Animals, Glass, Microscopy, Atomic Force.

Abstract

The high molecular mass respiratory protein of the tarantula Eurypelma californicum, a 4 x 6-mer hemocyanin, was investigated by atomic force microscopy (AFM). Various substrates and methods were evaluated for immobilization of individual hemocyanin molecules on a solid surface. Samples were imaged after physisorption on mica and self-assembled monolayers, and after chemisorption on Au(111) and N-hydroxy-succinimide (NHS) functionalized surfaces. AFM measurements were carried out preferable in solution and contact mode, but also in Tapping mode and on air-dried samples. Adsorption of the protein on mica followed by drying and carrying out the measurements in Tapping mode gave the best results. In the AFM images the four hexamers of the native 4 x 6-mer hemocyanin have been defined. The results were compared with independent available structural data and represent a validation case for this technique applied for the first time on such giant and complex molecules. As observable in images taken by transmission electron microscopy and also proposed from SAXS data, 4 x 6-mers could be found where the half-molecules are tilted against each other. This study is a step in resolving conformational heterogeneities, involved in oxygen binding of hemocyanins, at the single-molecule level by AFM.

DOI: 10.1016/j.micron.2006.03.003
PubMed: 16632369

Links to Exploration step

pubmed:16632369

Le document en format XML

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<author><name sortKey="Erker, Wolfgang" sort="Erker, Wolfgang" uniqKey="Erker W" first="Wolfgang" last="Erker">Wolfgang Erker</name>
<affiliation><nlm:affiliation>Institute for Physical Chemistry, University Mainz, Germany. erker@mail.uni-mainz.de</nlm:affiliation>
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<author><name sortKey="Scheumann, Volker" sort="Scheumann, Volker" uniqKey="Scheumann V" first="Volker" last="Scheumann">Volker Scheumann</name>
</author>
<author><name sortKey="Moller, Marco" sort="Moller, Marco" uniqKey="Moller M" first="Marco" last="Möller">Marco Möller</name>
</author>
<author><name sortKey="Knoll, Wolfgang" sort="Knoll, Wolfgang" uniqKey="Knoll W" first="Wolfgang" last="Knoll">Wolfgang Knoll</name>
</author>
<author><name sortKey="Ruhe, Jurgen" sort="Ruhe, Jurgen" uniqKey="Ruhe J" first="Jürgen" last="Rühe">Jürgen Rühe</name>
</author>
<author><name sortKey="Decker, Heinz" sort="Decker, Heinz" uniqKey="Decker H" first="Heinz" last="Decker">Heinz Decker</name>
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<author><name sortKey="Scheumann, Volker" sort="Scheumann, Volker" uniqKey="Scheumann V" first="Volker" last="Scheumann">Volker Scheumann</name>
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<author><name sortKey="Moller, Marco" sort="Moller, Marco" uniqKey="Moller M" first="Marco" last="Möller">Marco Möller</name>
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<series><title level="j">Micron (Oxford, England : 1993)</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Air</term>
<term>Aluminum Silicates</term>
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<term>Gold</term>
<term>Hemocyanins (isolation & purification)</term>
<term>Hemocyanins (ultrastructure)</term>
<term>Image Enhancement (methods)</term>
<term>Microscopy, Atomic Force</term>
<term>Preservation, Biological (methods)</term>
<term>Spiders (chemistry)</term>
<term>Succinimides</term>
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<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Hemocyanins</term>
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<keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Hemocyanins</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Aluminum Silicates</term>
<term>Gold</term>
<term>Succinimides</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Spiders</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Image Enhancement</term>
<term>Preservation, Biological</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Air</term>
<term>Animals</term>
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<front><div type="abstract" xml:lang="en">The high molecular mass respiratory protein of the tarantula Eurypelma californicum, a 4 x 6-mer hemocyanin, was investigated by atomic force microscopy (AFM). Various substrates and methods were evaluated for immobilization of individual hemocyanin molecules on a solid surface. Samples were imaged after physisorption on mica and self-assembled monolayers, and after chemisorption on Au(111) and N-hydroxy-succinimide (NHS) functionalized surfaces. AFM measurements were carried out preferable in solution and contact mode, but also in Tapping mode and on air-dried samples. Adsorption of the protein on mica followed by drying and carrying out the measurements in Tapping mode gave the best results. In the AFM images the four hexamers of the native 4 x 6-mer hemocyanin have been defined. The results were compared with independent available structural data and represent a validation case for this technique applied for the first time on such giant and complex molecules. As observable in images taken by transmission electron microscopy and also proposed from SAXS data, 4 x 6-mers could be found where the half-molecules are tilted against each other. This study is a step in resolving conformational heterogeneities, involved in oxygen binding of hemocyanins, at the single-molecule level by AFM.</div>
</front>
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<Title>Micron (Oxford, England : 1993)</Title>
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<ArticleTitle>Immobilization and AFM of single 4 x 6-mer tarantula hemocyanin molecules.</ArticleTitle>
<Pagination><MedlinePgn>735-41</MedlinePgn>
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<Abstract><AbstractText>The high molecular mass respiratory protein of the tarantula Eurypelma californicum, a 4 x 6-mer hemocyanin, was investigated by atomic force microscopy (AFM). Various substrates and methods were evaluated for immobilization of individual hemocyanin molecules on a solid surface. Samples were imaged after physisorption on mica and self-assembled monolayers, and after chemisorption on Au(111) and N-hydroxy-succinimide (NHS) functionalized surfaces. AFM measurements were carried out preferable in solution and contact mode, but also in Tapping mode and on air-dried samples. Adsorption of the protein on mica followed by drying and carrying out the measurements in Tapping mode gave the best results. In the AFM images the four hexamers of the native 4 x 6-mer hemocyanin have been defined. The results were compared with independent available structural data and represent a validation case for this technique applied for the first time on such giant and complex molecules. As observable in images taken by transmission electron microscopy and also proposed from SAXS data, 4 x 6-mers could be found where the half-molecules are tilted against each other. This study is a step in resolving conformational heterogeneities, involved in oxygen binding of hemocyanins, at the single-molecule level by AFM.</AbstractText>
</Abstract>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000388" MajorTopicYN="N">Air</DescriptorName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D013112" MajorTopicYN="N">Spiders</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013388" MajorTopicYN="N">Succinimides</DescriptorName>
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Immobilization and AFM of single 4 x 6-mer tarantula hemocyanin molecules.

Immobilization and AFM of single 4 x 6-mer tarantula hemocyanin molecules.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki