Mapping single molecular binding kinetics of carbohydrate-binding module with crystalline cellulose by atomic force microscopy recognition imaging.
Identifieur interne : 002142 ( Main/Exploration ); précédent : 002141; suivant : 002143Mapping single molecular binding kinetics of carbohydrate-binding module with crystalline cellulose by atomic force microscopy recognition imaging.
Auteurs : Mengmeng Zhang [États-Unis] ; Bin Wang ; Bingqian XuSource :
- The journal of physical chemistry. B [ 1520-5207 ] ; 2014.
Descripteurs français
- KwdFr :
- Cellulose (composition chimique), Cellulose (métabolisme), Cinétique (MeSH), Clostridium thermocellum (métabolisme), Liaison aux protéines (MeSH), Microscopie à force atomique (MeSH), Paroi cellulaire (métabolisme), Plantes (métabolisme), Protéines bactériennes (composition chimique), Protéines bactériennes (métabolisme), Sites de fixation (MeSH), Structure tertiaire des protéines (MeSH).
- MESH :
- composition chimique : Cellulose, Protéines bactériennes.
- métabolisme : Cellulose, Clostridium thermocellum, Paroi cellulaire, Plantes, Protéines bactériennes.
- Cinétique, Liaison aux protéines, Microscopie à force atomique, Sites de fixation, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Binding Sites (MeSH), Cell Wall (metabolism), Cellulose (chemistry), Cellulose (metabolism), Clostridium thermocellum (metabolism), Kinetics (MeSH), Microscopy, Atomic Force (MeSH), Plants (metabolism), Protein Binding (MeSH), Protein Structure, Tertiary (MeSH).
- MESH :
- chemical , chemistry : Bacterial Proteins, Cellulose.
- chemical , metabolism : Bacterial Proteins, Cellulose.
- metabolism : Cell Wall, Clostridium thermocellum, Plants.
- Binding Sites, Kinetics, Microscopy, Atomic Force, Protein Binding, Protein Structure, Tertiary.
Abstract
We studied the binding kinetics of family 3 carbohydrate-binding module (CBM3a) molecules to crystalline cellulose fibrils extracted from the poplar cell wall by atomic force microscopy (AFM) recognition imaging. The free CBM3a molecules of different concentrations were added to the buffer solution to bind to the crystalline cellulose sample immobilized on the AFM substrate. During in-situ AFM imaging, the CBM molecules were observed to bind to cellulose efficiently and regularly, especially in the first 60-120 min. A 1:1 single-molecule binding model was used to study the kinetics of the CBM3a-cellulose interaction. The saturation time when the concentration of occupied binding sites is 99% of the maximum bound CBM3a concentration at the end of reaction, t(0.99), was determined by fitting different concentrations of CBM3a against reaction time using the high resolution AFM images and the single-molecule kinetics equations. Based on the experimental data and kinetics calculations, the minimal effective initial CBM3a concentration was estimated to be 5.1 × 10(-7) M at 287 min reaction time. This study provides an in-depth understanding of the binding mechanism of CBM with crystalline cellulose at single molecule level.
DOI: 10.1021/jp503185n
PubMed: 24878225
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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B</title><idno type="eISSN">1520-5207</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (metabolism)</term><term>Binding Sites (MeSH)</term><term>Cell Wall (metabolism)</term><term>Cellulose (chemistry)</term><term>Cellulose (metabolism)</term><term>Clostridium thermocellum (metabolism)</term><term>Kinetics (MeSH)</term><term>Microscopy, Atomic Force (MeSH)</term><term>Plants (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellulose (composition chimique)</term><term>Cellulose (métabolisme)</term><term>Cinétique (MeSH)</term><term>Clostridium thermocellum (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Microscopie à force atomique (MeSH)</term><term>Paroi cellulaire (métabolisme)</term><term>Plantes (métabolisme)</term><term>Protéines bactériennes (composition chimique)</term><term>Protéines bactériennes (métabolisme)</term><term>Sites de fixation (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>Cellulose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Cellulose</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellulose</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Wall</term><term>Clostridium thermocellum</term><term>Plants</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellulose</term><term>Clostridium thermocellum</term><term>Paroi cellulaire</term><term>Plantes</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Kinetics</term><term>Microscopy, Atomic Force</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Liaison aux protéines</term><term>Microscopie à force atomique</term><term>Sites de fixation</term><term>Structure tertiaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We studied the binding kinetics of family 3 carbohydrate-binding module (CBM3a) molecules to crystalline cellulose fibrils extracted from the poplar cell wall by atomic force microscopy (AFM) recognition imaging. The free CBM3a molecules of different concentrations were added to the buffer solution to bind to the crystalline cellulose sample immobilized on the AFM substrate. During in-situ AFM imaging, the CBM molecules were observed to bind to cellulose efficiently and regularly, especially in the first 60-120 min. A 1:1 single-molecule binding model was used to study the kinetics of the CBM3a-cellulose interaction. The saturation time when the concentration of occupied binding sites is 99% of the maximum bound CBM3a concentration at the end of reaction, t(0.99), was determined by fitting different concentrations of CBM3a against reaction time using the high resolution AFM images and the single-molecule kinetics equations. Based on the experimental data and kinetics calculations, the minimal effective initial CBM3a concentration was estimated to be 5.1 × 10(-7) M at 287 min reaction time. This study provides an in-depth understanding of the binding mechanism of CBM with crystalline cellulose at single molecule level. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24878225</PMID><DateCompleted><Year>2015</Year><Month>05</Month><Day>18</Day></DateCompleted><DateRevised><Year>2014</Year><Month>06</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5207</ISSN><JournalIssue CitedMedium="Internet"><Volume>118</Volume><Issue>24</Issue><PubDate><Year>2014</Year><Month>Jun</Month><Day>19</Day></PubDate></JournalIssue><Title>The journal of physical chemistry. B</Title><ISOAbbreviation>J Phys Chem B</ISOAbbreviation></Journal><ArticleTitle>Mapping single molecular binding kinetics of carbohydrate-binding module with crystalline cellulose by atomic force microscopy recognition imaging.</ArticleTitle><Pagination><MedlinePgn>6714-20</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/jp503185n</ELocationID><Abstract><AbstractText>We studied the binding kinetics of family 3 carbohydrate-binding module (CBM3a) molecules to crystalline cellulose fibrils extracted from the poplar cell wall by atomic force microscopy (AFM) recognition imaging. The free CBM3a molecules of different concentrations were added to the buffer solution to bind to the crystalline cellulose sample immobilized on the AFM substrate. During in-situ AFM imaging, the CBM molecules were observed to bind to cellulose efficiently and regularly, especially in the first 60-120 min. A 1:1 single-molecule binding model was used to study the kinetics of the CBM3a-cellulose interaction. The saturation time when the concentration of occupied binding sites is 99% of the maximum bound CBM3a concentration at the end of reaction, t(0.99), was determined by fitting different concentrations of CBM3a against reaction time using the high resolution AFM images and the single-molecule kinetics equations. Based on the experimental data and kinetics calculations, the minimal effective initial CBM3a concentration was estimated to be 5.1 × 10(-7) M at 287 min reaction time. This study provides an in-depth understanding of the binding mechanism of CBM with crystalline cellulose at single molecule level. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Mengmeng</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Single Molecule Study Laboratory, College of Engineering and Nanoscale Science and Engineering Center, University of Georgia , Athens, Georgia 30602, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Bin</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>Bingqian</ForeName><Initials>B</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>06</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Phys Chem B</MedlineTA><NlmUniqueID>101157530</NlmUniqueID><ISSNLinking>1520-5207</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9004-34-6</RegistryNumber><NameOfSubstance UI="D002482">Cellulose</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002473" MajorTopicYN="N">Cell Wall</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002482" MajorTopicYN="N">Cellulose</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D048013" MajorTopicYN="N">Clostridium thermocellum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018625" MajorTopicYN="Y">Microscopy, Atomic Force</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>6</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>6</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>5</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24878225</ArticleId><ArticleId IdType="doi">10.1021/jp503185n</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Wang, Bin" sort="Wang, Bin" uniqKey="Wang B" first="Bin" last="Wang">Bin Wang</name><name sortKey="Xu, Bingqian" sort="Xu, Bingqian" uniqKey="Xu B" first="Bingqian" last="Xu">Bingqian Xu</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Zhang, Mengmeng" sort="Zhang, Mengmeng" uniqKey="Zhang M" first="Mengmeng" last="Zhang">Mengmeng Zhang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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