Imaging and measuring single-molecule interaction between a carbohydrate-binding module and natural plant cell wall cellulose.
Identifieur interne : 002A34 ( Main/Exploration ); précédent : 002A33; suivant : 002A35Imaging and measuring single-molecule interaction between a carbohydrate-binding module and natural plant cell wall cellulose.
Auteurs : Mengmeng Zhang [États-Unis] ; Sheng-Cheng Wu ; Wen Zhou ; Bingqian XuSource :
- The journal of physical chemistry. B [ 1520-5207 ] ; 2012.
Descripteurs français
- KwdFr :
- Cellulose (composition chimique), Clostridium thermocellum (composition chimique), Clostridium thermocellum (génétique), Glucides (composition chimique), Nanoparticules métalliques (composition chimique), Or (composition chimique), Paroi cellulaire (composition chimique), Populus (composition chimique), Populus (cytologie), Propriétés de surface (MeSH), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Sites de fixation (MeSH).
- MESH :
- composition chimique : Cellulose, Clostridium thermocellum, Glucides, Nanoparticules métalliques, Or, Paroi cellulaire, Populus, Protéines recombinantes.
- cytologie : Populus.
- génétique : Clostridium thermocellum, Protéines recombinantes.
- Propriétés de surface, Sites de fixation.
English descriptors
- KwdEn :
- Binding Sites (MeSH), Carbohydrates (chemistry), Cell Wall (chemistry), Cellulose (chemistry), Clostridium thermocellum (chemistry), Clostridium thermocellum (genetics), Gold (chemistry), Metal Nanoparticles (chemistry), Populus (chemistry), Populus (cytology), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Surface Properties (MeSH).
- MESH :
- chemical , chemistry : Carbohydrates, Cellulose, Gold, Recombinant Proteins.
- chemistry : Cell Wall, Clostridium thermocellum, Metal Nanoparticles, Populus.
- cytology : Populus.
- genetics : Clostridium thermocellum, Recombinant Proteins.
- Binding Sites, Surface Properties.
Abstract
The affinitive interaction between a carbohydrate-binding module (CBM3a) and natural crystalline cellulose was visualized and measured at the single-molecule level. Noncontact high resolution imaging by atomic force microscopy (AFM) was used to follow the binding process, in real time, of CBM3a-functionalized 6 nm gold nanoparticles (GNPs) to the cell wall polymers on poplar stem sections. The GNP-CBM3a complexes were found to bind to the cellulose surface, closely aligning along the cellulose fibril axis. The binding details were further confirmed and studied by single-molecule recognition imaging and AFM single-molecule dynamic force spectroscopy (SMDFS) using a CBM3a-functionalized AFM tip. The unbinding force was measured to be 44.96 ± 18.80 pN under a loading rate of 67.2 nN/s. This research provides a radical method for the study of single-molecule affinity between CBM and cellulose that is critical to the engineering of novel cellulolytic enzymes.
DOI: 10.1021/jp304686q
PubMed: 22849362
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<author><name sortKey="Zhou, Wen" sort="Zhou, Wen" uniqKey="Zhou W" first="Wen" last="Zhou">Wen Zhou</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term>
<term>Carbohydrates (chemistry)</term>
<term>Cell Wall (chemistry)</term>
<term>Cellulose (chemistry)</term>
<term>Clostridium thermocellum (chemistry)</term>
<term>Clostridium thermocellum (genetics)</term>
<term>Gold (chemistry)</term>
<term>Metal Nanoparticles (chemistry)</term>
<term>Populus (chemistry)</term>
<term>Populus (cytology)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Surface Properties (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Cellulose (composition chimique)</term>
<term>Clostridium thermocellum (composition chimique)</term>
<term>Clostridium thermocellum (génétique)</term>
<term>Glucides (composition chimique)</term>
<term>Nanoparticules métalliques (composition chimique)</term>
<term>Or (composition chimique)</term>
<term>Paroi cellulaire (composition chimique)</term>
<term>Populus (composition chimique)</term>
<term>Populus (cytologie)</term>
<term>Propriétés de surface (MeSH)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Sites de fixation (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carbohydrates</term>
<term>Cellulose</term>
<term>Gold</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Wall</term>
<term>Clostridium thermocellum</term>
<term>Metal Nanoparticles</term>
<term>Populus</term>
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<term>Clostridium thermocellum</term>
<term>Glucides</term>
<term>Nanoparticules métalliques</term>
<term>Or</term>
<term>Paroi cellulaire</term>
<term>Populus</term>
<term>Protéines recombinantes</term>
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<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Populus</term>
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<term>Surface Properties</term>
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<front><div type="abstract" xml:lang="en">The affinitive interaction between a carbohydrate-binding module (CBM3a) and natural crystalline cellulose was visualized and measured at the single-molecule level. Noncontact high resolution imaging by atomic force microscopy (AFM) was used to follow the binding process, in real time, of CBM3a-functionalized 6 nm gold nanoparticles (GNPs) to the cell wall polymers on poplar stem sections. The GNP-CBM3a complexes were found to bind to the cellulose surface, closely aligning along the cellulose fibril axis. The binding details were further confirmed and studied by single-molecule recognition imaging and AFM single-molecule dynamic force spectroscopy (SMDFS) using a CBM3a-functionalized AFM tip. The unbinding force was measured to be 44.96 ± 18.80 pN under a loading rate of 67.2 nN/s. This research provides a radical method for the study of single-molecule affinity between CBM and cellulose that is critical to the engineering of novel cellulolytic enzymes.</div>
</front>
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<Abstract><AbstractText>The affinitive interaction between a carbohydrate-binding module (CBM3a) and natural crystalline cellulose was visualized and measured at the single-molecule level. Noncontact high resolution imaging by atomic force microscopy (AFM) was used to follow the binding process, in real time, of CBM3a-functionalized 6 nm gold nanoparticles (GNPs) to the cell wall polymers on poplar stem sections. The GNP-CBM3a complexes were found to bind to the cellulose surface, closely aligning along the cellulose fibril axis. The binding details were further confirmed and studied by single-molecule recognition imaging and AFM single-molecule dynamic force spectroscopy (SMDFS) using a CBM3a-functionalized AFM tip. The unbinding force was measured to be 44.96 ± 18.80 pN under a loading rate of 67.2 nN/s. This research provides a radical method for the study of single-molecule affinity between CBM and cellulose that is critical to the engineering of novel cellulolytic enzymes.</AbstractText>
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