Effects of macromolecular crowding on the collapse of biopolymers
Experiments show that macromolecular crowding modestly reduces the size of intrinsically disordered proteins even at a volume fraction (ϕ) similar to that in the cytosol, whereas DNA undergoes a coil-to-globule transition at very small ϕ. We show using a combination of scaling arguments and simulati...
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| Veröffentlicht in: | Physical review letters 2015-02, Vol.114 (6), p.068303-068303, Article 068303 |
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| creator | Kang, Hongsuk Pincus, Philip A Hyeon, Changbong Thirumalai, D |
| description | Experiments show that macromolecular crowding modestly reduces the size of intrinsically disordered proteins even at a volume fraction (ϕ) similar to that in the cytosol, whereas DNA undergoes a coil-to-globule transition at very small ϕ. We show using a combination of scaling arguments and simulations that the polymer size R̅(g)(ϕ) depends on x=R̅(g)(0)/D, where D is the ϕ-dependent distance between the crowders. If x≲O(1), there is only a small decrease in R̅(g)(ϕ) as ϕ increases. When x≫O(1), a cooperative coil-to-globule transition is induced. Our theory quantitatively explains a number of experiments. |
| doi_str_mv | 10.1103/physrevlett.114.068303 |
| format | Article |
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Our theory quantitatively explains a number of experiments.</description><subject>Biopolymers</subject><subject>Coiling</subject><subject>Collapse</subject><subject>Computer Simulation</subject><subject>Crowding</subject><subject>Deoxyribonucleic acid</subject><subject>DNA - chemistry</subject><subject>Macromolecular Substances - chemistry</subject><subject>Models, Chemical</subject><subject>Nucleic Acid Conformation</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Simulation</subject><subject>Volume fraction</subject><issn>0031-9007</issn><issn>1079-7114</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0EoqXwC1WWbFLGdmzHy6oqD6kSCHUfOcmYBiV1iJOi_D2uWtiyGs3VvfM4hMwpLCgF_tDuRt_hoca-D0KyAJly4BdkSkHpWAXpkkwBOI01gJqQG-8_AYAymV6TCROKcZboKVmurcWi95GzUWOKzjWuxmKoTReF5rus9h-R20f9DqPC1bVpPR6teeVaV48Ndv6WXFlTe7w71xnZPq63q-d48_r0slpu4kJQ2sdCS5MrSAVIoXgKRnNrrdSJVbpkCGgpWCPKVLJSgmCYm1xQQQsUMk0SPiP3p7Ft574G9H3WVL7AcNIe3eAzqlJJFVdS_2-VMpBhCT1a5ckanvUBqM3armpMN2YUsiPo7C2AfsfDJoAOQpKdQIfg_LxjyBss_2K_ZPkPVkl8Bg</recordid><startdate>20150213</startdate><enddate>20150213</enddate><creator>Kang, Hongsuk</creator><creator>Pincus, Philip A</creator><creator>Hyeon, Changbong</creator><creator>Thirumalai, D</creator><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>7U5</scope><scope>8FD</scope><scope>H8D</scope><scope>L7M</scope></search><sort><creationdate>20150213</creationdate><title>Effects of macromolecular crowding on the collapse of biopolymers</title><author>Kang, Hongsuk ; Pincus, Philip A ; Hyeon, Changbong ; Thirumalai, D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c511t-596ab70850657380a93fff694f79d2e0ef10fa5d862d6052ebab5151ce568443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Biopolymers</topic><topic>Coiling</topic><topic>Collapse</topic><topic>Computer Simulation</topic><topic>Crowding</topic><topic>Deoxyribonucleic acid</topic><topic>DNA - chemistry</topic><topic>Macromolecular Substances - chemistry</topic><topic>Models, Chemical</topic><topic>Nucleic Acid Conformation</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Simulation</topic><topic>Volume fraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kang, Hongsuk</creatorcontrib><creatorcontrib>Pincus, Philip A</creatorcontrib><creatorcontrib>Hyeon, Changbong</creatorcontrib><creatorcontrib>Thirumalai, D</creatorcontrib><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>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Aerospace Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Physical review letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kang, Hongsuk</au><au>Pincus, Philip A</au><au>Hyeon, Changbong</au><au>Thirumalai, D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of macromolecular crowding on the collapse of biopolymers</atitle><jtitle>Physical review letters</jtitle><addtitle>Phys Rev Lett</addtitle><date>2015-02-13</date><risdate>2015</risdate><volume>114</volume><issue>6</issue><spage>068303</spage><epage>068303</epage><pages>068303-068303</pages><artnum>068303</artnum><issn>0031-9007</issn><eissn>1079-7114</eissn><abstract>Experiments show that macromolecular crowding modestly reduces the size of intrinsically disordered proteins even at a volume fraction (ϕ) similar to that in the cytosol, whereas DNA undergoes a coil-to-globule transition at very small ϕ. 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| subjects | Biopolymers Coiling Collapse Computer Simulation Crowding Deoxyribonucleic acid DNA - chemistry Macromolecular Substances - chemistry Models, Chemical Nucleic Acid Conformation Protein Conformation Proteins Proteins - chemistry Simulation Volume fraction |
| title | Effects of macromolecular crowding on the collapse of biopolymers |
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