Physics of actin networks. I. Rheology of semi-dilute F-actin
The mechanical properties of cytoplasm are considered to be of underlying importance in the mechanism of cell movement and are to a large extent determined by an actin-containing cytoskeleton. Several laboratories have begun to accumulate data on the mechanical or rheologic properties of protein sys...
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Veröffentlicht in: | Biophysical journal 1995-03, Vol.68 (3), p.1019-1026 |
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description | The mechanical properties of cytoplasm are considered to be of underlying importance in the mechanism of cell movement and are to a large extent determined by an actin-containing cytoskeleton. Several laboratories have begun to accumulate data on the mechanical or rheologic properties of protein systems derived from the actin cytoskeleton. The focus of this manuscript is to attempt to reproduce the experimentally determined mechanical properties of non-cross-linked F-actin from theoretical considerations. It was found that a mechanical spectrum for 1 mg/ml F-actin could be calculated, which approximated experimental data, from a relaxation spectrum consisting of a long range rotational diffusion motion and short range bending motion, assuming an exponential distribution of filament lengths with a weight average length of 4 mu. The calculated spectrum underestimated the dynamic moduli at high frequencies, suggesting that a more complex actin structure is present that enhances the high frequency component. |
doi_str_mv | 10.1016/S0006-3495(95)80277-8 |
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It was found that a mechanical spectrum for 1 mg/ml F-actin could be calculated, which approximated experimental data, from a relaxation spectrum consisting of a long range rotational diffusion motion and short range bending motion, assuming an exponential distribution of filament lengths with a weight average length of 4 mu. 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I. Rheology of semi-dilute F-actin</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>The mechanical properties of cytoplasm are considered to be of underlying importance in the mechanism of cell movement and are to a large extent determined by an actin-containing cytoskeleton. Several laboratories have begun to accumulate data on the mechanical or rheologic properties of protein systems derived from the actin cytoskeleton. The focus of this manuscript is to attempt to reproduce the experimentally determined mechanical properties of non-cross-linked F-actin from theoretical considerations. It was found that a mechanical spectrum for 1 mg/ml F-actin could be calculated, which approximated experimental data, from a relaxation spectrum consisting of a long range rotational diffusion motion and short range bending motion, assuming an exponential distribution of filament lengths with a weight average length of 4 mu. The calculated spectrum underestimated the dynamic moduli at high frequencies, suggesting that a more complex actin structure is present that enhances the high frequency component.</description><subject>Actins - chemistry</subject><subject>Actins - physiology</subject><subject>Animals</subject><subject>Biomechanical Phenomena</subject><subject>Biophysical Phenomena</subject><subject>Biophysics</subject><subject>Cell Movement - physiology</subject><subject>Cytoskeleton - chemistry</subject><subject>Cytoskeleton - physiology</subject><subject>In Vitro Techniques</subject><subject>Muscle, Skeletal - chemistry</subject><subject>Rabbits</subject><subject>Rheology</subject><subject>Solutions</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtKAzEUhoMotVYfoTAr0cXUXJpJZqEixWqhoHhZh0zmTBudTmoyrfTtnV4ouhICWfzf-c_hQ6hLcI9gkly9YoyTmPVTfpHyS4mpELE8QG3C-zTGWCaHqL1HjtFJCB8YE8oxaaGWEDzhlLbR9fN0FawJkSsibWpbRRXU385_hl406kUvU3Clm6zWcYCZjXNbLmqIhvEGPkVHhS4DnO3-Dnof3r8NHuPx08NocDeODRNCxhJSYbhMmZCYCZIlvEh5lkPCRCGzLKeEccEhJ0WWakETLRKW9lmW0j5lWgProJtt73yRzSA3UNVel2ru7Uz7lXLaqr9JZadq4paKUEkk5U3B-a7Au68FhFrNbDBQlroCtwhKiAZkfA3yLWi8C8FDsV9CsFp7Vxvvai1VNW_jXclmrvv7wv3UTnST325zaDQtLXgVjIXKQG49mFrlzv6z4Qc685Ge</recordid><startdate>19950301</startdate><enddate>19950301</enddate><creator>Zaner, K.S.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19950301</creationdate><title>Physics of actin networks. I. Rheology of semi-dilute F-actin</title><author>Zaner, K.S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3778-8e97c5893780371b65f95bde637f8bbd213575ed1fb9a726a763943b92423aae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Actins - chemistry</topic><topic>Actins - physiology</topic><topic>Animals</topic><topic>Biomechanical Phenomena</topic><topic>Biophysical Phenomena</topic><topic>Biophysics</topic><topic>Cell Movement - physiology</topic><topic>Cytoskeleton - chemistry</topic><topic>Cytoskeleton - physiology</topic><topic>In Vitro Techniques</topic><topic>Muscle, Skeletal - chemistry</topic><topic>Rabbits</topic><topic>Rheology</topic><topic>Solutions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zaner, K.S.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zaner, K.S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Physics of actin networks. I. Rheology of semi-dilute F-actin</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1995-03-01</date><risdate>1995</risdate><volume>68</volume><issue>3</issue><spage>1019</spage><epage>1026</epage><pages>1019-1026</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>The mechanical properties of cytoplasm are considered to be of underlying importance in the mechanism of cell movement and are to a large extent determined by an actin-containing cytoskeleton. Several laboratories have begun to accumulate data on the mechanical or rheologic properties of protein systems derived from the actin cytoskeleton. The focus of this manuscript is to attempt to reproduce the experimentally determined mechanical properties of non-cross-linked F-actin from theoretical considerations. It was found that a mechanical spectrum for 1 mg/ml F-actin could be calculated, which approximated experimental data, from a relaxation spectrum consisting of a long range rotational diffusion motion and short range bending motion, assuming an exponential distribution of filament lengths with a weight average length of 4 mu. The calculated spectrum underestimated the dynamic moduli at high frequencies, suggesting that a more complex actin structure is present that enhances the high frequency component.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7756522</pmid><doi>10.1016/S0006-3495(95)80277-8</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Actins - chemistry Actins - physiology Animals Biomechanical Phenomena Biophysical Phenomena Biophysics Cell Movement - physiology Cytoskeleton - chemistry Cytoskeleton - physiology In Vitro Techniques Muscle, Skeletal - chemistry Rabbits Rheology Solutions |
title | Physics of actin networks. I. Rheology of semi-dilute F-actin |
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