Direct quantification of the flexibility of type I collagen monomer
Collagens are the most abundant structural proteins found in the extracellular matrix of vertebrates. Knowledge of the mechanical behavior of collagen monomers is essential for understanding the mechanical properties of collagen fibrils that constitute the main architectural framework of skin, bone,...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2002-07, Vol.295 (2), p.382-386 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 386 |
|---|---|
| container_issue | 2 |
| container_start_page | 382 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 295 |
| creator | Sun, Yu-Long Luo, Zong-Ping Fertala, Andrzej An, Kai-Nan |
| description | Collagens are the most abundant structural proteins found in the extracellular matrix of vertebrates. Knowledge of the mechanical behavior of collagen monomers is essential for understanding the mechanical properties of collagen fibrils that constitute the main architectural framework of skin, bone, cartilage, and other connective tissues. In this study, the flexibility of type I collagen monomer was studied by stretching type I collagen monomers directly. The force–extension relationship was measured and analyzed by fitting the data into a worm-like chain elasticity model. The persistence length of collagen I monomer was determined to be 14.5
nm and the contour length was 309
nm. The results comfirm that type I collagen monomer is flexible rather than rigid, rod-like molecule. Such flexibility may possibly be a consequence of the micro-unfolding of discrete domains of single collagen molecule. |
| doi_str_mv | 10.1016/S0006-291X(02)00685-X |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71981915</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X0200685X</els_id><sourcerecordid>18580107</sourcerecordid><originalsourceid>FETCH-LOGICAL-c458t-da8003bda2a1e40552d006ef173c9dc9e2863d3add528a5f605920f24e6692683</originalsourceid><addsrcrecordid>eNqFkE1v2zAMhoVhxZJm-wkrfBrWgztSthTpVBTpV4AAPWwDchMUid5U2FZqOUPz7-d8oD3mRIJ4SL54GPuKcIWA8sdPAJA517j8Dvxy6JXIlx_YGEFDzhHKj2z8hozYeUrPAIil1J_YCDkK0BLGbHYbOnJ99rKxbR-q4GwfYpvFKuv_UlbV9BpWoQ79dj_arimbZy7Wtf1DbdbENjbUfWZnla0TfTnWCft9f_dr9pgvnh7ms5tF7kqh-txbBVCsvOUWqQQhuB_yUYXTwmnvNHElC19Y7wVXVlQShOZQ8ZKk1FyqYsK-He6uu_iyodSbJiRHQ5iW4iaZKWqFGsVJEJVQgDAdQHEAXRdT6qgy6y40ttsaBLPTbPaazc6hAW72ms1y2Ls4PtisGvLvW0evA3B9AGjw8S9QZ5IL1Drye93Gx3DixX8Sa4wx</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18580107</pqid></control><display><type>article</type><title>Direct quantification of the flexibility of type I collagen monomer</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Sun, Yu-Long ; Luo, Zong-Ping ; Fertala, Andrzej ; An, Kai-Nan</creator><creatorcontrib>Sun, Yu-Long ; Luo, Zong-Ping ; Fertala, Andrzej ; An, Kai-Nan</creatorcontrib><description>Collagens are the most abundant structural proteins found in the extracellular matrix of vertebrates. Knowledge of the mechanical behavior of collagen monomers is essential for understanding the mechanical properties of collagen fibrils that constitute the main architectural framework of skin, bone, cartilage, and other connective tissues. In this study, the flexibility of type I collagen monomer was studied by stretching type I collagen monomers directly. The force–extension relationship was measured and analyzed by fitting the data into a worm-like chain elasticity model. The persistence length of collagen I monomer was determined to be 14.5
nm and the contour length was 309
nm. The results comfirm that type I collagen monomer is flexible rather than rigid, rod-like molecule. Such flexibility may possibly be a consequence of the micro-unfolding of discrete domains of single collagen molecule.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(02)00685-X</identifier><identifier>PMID: 12150960</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Collagen Type I - chemistry ; Flexibility ; Humans ; Nanotechnology ; Optical tweezers ; Persistence length ; Protein Conformation ; Type I collagen</subject><ispartof>Biochemical and biophysical research communications, 2002-07, Vol.295 (2), p.382-386</ispartof><rights>2002 Elsevier Science (USA)</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-da8003bda2a1e40552d006ef173c9dc9e2863d3add528a5f605920f24e6692683</citedby><cites>FETCH-LOGICAL-c458t-da8003bda2a1e40552d006ef173c9dc9e2863d3add528a5f605920f24e6692683</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-291X(02)00685-X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12150960$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sun, Yu-Long</creatorcontrib><creatorcontrib>Luo, Zong-Ping</creatorcontrib><creatorcontrib>Fertala, Andrzej</creatorcontrib><creatorcontrib>An, Kai-Nan</creatorcontrib><title>Direct quantification of the flexibility of type I collagen monomer</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Collagens are the most abundant structural proteins found in the extracellular matrix of vertebrates. Knowledge of the mechanical behavior of collagen monomers is essential for understanding the mechanical properties of collagen fibrils that constitute the main architectural framework of skin, bone, cartilage, and other connective tissues. In this study, the flexibility of type I collagen monomer was studied by stretching type I collagen monomers directly. The force–extension relationship was measured and analyzed by fitting the data into a worm-like chain elasticity model. The persistence length of collagen I monomer was determined to be 14.5
nm and the contour length was 309
nm. The results comfirm that type I collagen monomer is flexible rather than rigid, rod-like molecule. Such flexibility may possibly be a consequence of the micro-unfolding of discrete domains of single collagen molecule.</description><subject>Collagen Type I - chemistry</subject><subject>Flexibility</subject><subject>Humans</subject><subject>Nanotechnology</subject><subject>Optical tweezers</subject><subject>Persistence length</subject><subject>Protein Conformation</subject><subject>Type I collagen</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1v2zAMhoVhxZJm-wkrfBrWgztSthTpVBTpV4AAPWwDchMUid5U2FZqOUPz7-d8oD3mRIJ4SL54GPuKcIWA8sdPAJA517j8Dvxy6JXIlx_YGEFDzhHKj2z8hozYeUrPAIil1J_YCDkK0BLGbHYbOnJ99rKxbR-q4GwfYpvFKuv_UlbV9BpWoQ79dj_arimbZy7Wtf1DbdbENjbUfWZnla0TfTnWCft9f_dr9pgvnh7ms5tF7kqh-txbBVCsvOUWqQQhuB_yUYXTwmnvNHElC19Y7wVXVlQShOZQ8ZKk1FyqYsK-He6uu_iyodSbJiRHQ5iW4iaZKWqFGsVJEJVQgDAdQHEAXRdT6qgy6y40ttsaBLPTbPaazc6hAW72ms1y2Ls4PtisGvLvW0evA3B9AGjw8S9QZ5IL1Drye93Gx3DixX8Sa4wx</recordid><startdate>20020712</startdate><enddate>20020712</enddate><creator>Sun, Yu-Long</creator><creator>Luo, Zong-Ping</creator><creator>Fertala, Andrzej</creator><creator>An, Kai-Nan</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7X8</scope></search><sort><creationdate>20020712</creationdate><title>Direct quantification of the flexibility of type I collagen monomer</title><author>Sun, Yu-Long ; Luo, Zong-Ping ; Fertala, Andrzej ; An, Kai-Nan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c458t-da8003bda2a1e40552d006ef173c9dc9e2863d3add528a5f605920f24e6692683</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Collagen Type I - chemistry</topic><topic>Flexibility</topic><topic>Humans</topic><topic>Nanotechnology</topic><topic>Optical tweezers</topic><topic>Persistence length</topic><topic>Protein Conformation</topic><topic>Type I collagen</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sun, Yu-Long</creatorcontrib><creatorcontrib>Luo, Zong-Ping</creatorcontrib><creatorcontrib>Fertala, Andrzej</creatorcontrib><creatorcontrib>An, Kai-Nan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sun, Yu-Long</au><au>Luo, Zong-Ping</au><au>Fertala, Andrzej</au><au>An, Kai-Nan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Direct quantification of the flexibility of type I collagen monomer</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2002-07-12</date><risdate>2002</risdate><volume>295</volume><issue>2</issue><spage>382</spage><epage>386</epage><pages>382-386</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Collagens are the most abundant structural proteins found in the extracellular matrix of vertebrates. Knowledge of the mechanical behavior of collagen monomers is essential for understanding the mechanical properties of collagen fibrils that constitute the main architectural framework of skin, bone, cartilage, and other connective tissues. In this study, the flexibility of type I collagen monomer was studied by stretching type I collagen monomers directly. The force–extension relationship was measured and analyzed by fitting the data into a worm-like chain elasticity model. The persistence length of collagen I monomer was determined to be 14.5
nm and the contour length was 309
nm. The results comfirm that type I collagen monomer is flexible rather than rigid, rod-like molecule. Such flexibility may possibly be a consequence of the micro-unfolding of discrete domains of single collagen molecule.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12150960</pmid><doi>10.1016/S0006-291X(02)00685-X</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2002-07, Vol.295 (2), p.382-386 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71981915 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Collagen Type I - chemistry Flexibility Humans Nanotechnology Optical tweezers Persistence length Protein Conformation Type I collagen |
| title | Direct quantification of the flexibility of type I collagen monomer |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T00%3A11%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Direct%20quantification%20of%20the%20flexibility%20of%20type%20I%20collagen%20monomer&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Sun,%20Yu-Long&rft.date=2002-07-12&rft.volume=295&rft.issue=2&rft.spage=382&rft.epage=386&rft.pages=382-386&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/S0006-291X(02)00685-X&rft_dat=%3Cproquest_cross%3E18580107%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=18580107&rft_id=info:pmid/12150960&rft_els_id=S0006291X0200685X&rfr_iscdi=true |