Loading…
Macromolecular Crowding and Intrinsically Disordered Proteins: A Polymer Physics Perspective
The cell is a crowded environment where a relevant fraction of the available space is occupied by proteins, nucleic acids, and metabolites. Here we discuss recent advancements in the understanding of crowding effects on intrinsically disordered proteins. Differently from their structured counterpart...
Saved in:
Published in: | ChemSystemsChem 2022-09, Vol.4 (5), p.n/a |
---|---|
Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c3171-4bb5066d61a0974c03d36b03ba048c0c325f7eba7da46ec8a21bedf3ffe4325b3 |
---|---|
cites | cdi_FETCH-LOGICAL-c3171-4bb5066d61a0974c03d36b03ba048c0c325f7eba7da46ec8a21bedf3ffe4325b3 |
container_end_page | n/a |
container_issue | 5 |
container_start_page | |
container_title | ChemSystemsChem |
container_volume | 4 |
creator | Cubuk, Jasmine Soranno, Andrea |
description | The cell is a crowded environment where a relevant fraction of the available space is occupied by proteins, nucleic acids, and metabolites. Here we discuss recent advancements in the understanding of crowding effects on intrinsically disordered proteins. Differently from their structured counterparts, these proteins do not adopt a stable three‐dimensional structure and remain flexible and dynamic in solution. The physics of polymers and colloids provides a framework to interpret how crowding modulates conformations, dynamics, and interactions of disordered proteins. Flory‐Huggins models enable rationalizing the different degree of compaction induced by crowding agents in terms of depletion interactions. The same interactions modulate the diffusion of the disordered proteins in a crowded milieu and the association and dissociation rates when interacting with a ligand. Altogether, this theoretical framework provides new insights into the interpretation of the effects of the cellular environment on disordered proteins.
The cell is a crowded environment where a relevant fraction of the available space is occupied. Intrinsically disordered proteins do not adopt a stable three‐dimensional structure and therefore are particularly sensitive to such crowded cellular milieu. This Review discusses how the physics of polymers and colloids provides a framework to interpret how crowding modulates conformations and interactions of disordered proteins. |
doi_str_mv | 10.1002/syst.202100051 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_2714172057</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2714172057</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3171-4bb5066d61a0974c03d36b03ba048c0c325f7eba7da46ec8a21bedf3ffe4325b3</originalsourceid><addsrcrecordid>eNqFkM1LAzEQxYMoWLRXzwHPrZNkd9N6K_WrUHGh9SAIIZvM6pbtpiZby_73plTUm6eZ4f3eDPMIuWAwZAD8KnShHXLgcYCUHZEeTyUMEg7Z8Z_-lPRDWEWEp0ywseyR10dtvFu7Gs221p5OvdvZqnmjurF01rS-akJldF139KYKzlv0aGnuXYtRuaYTmru6W6On-XsXyUBz9GGDpq0-8ZyclLoO2P-uZ-T57nY5fRjMn-5n08l8YASTbJAURQpZZjOmYSwTA8KKrABRaEhGBozgaSmx0NLqJEMz0pwVaEtRlphErRBn5PKwd-PdxxZDq1Zu65t4UnHJEiY5pDJSwwMVHw7BY6k2vlpr3ykGah-i2oeofkKMhvHBsKtq7P6h1eJlsfz1fgH3cXd7</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2714172057</pqid></control><display><type>article</type><title>Macromolecular Crowding and Intrinsically Disordered Proteins: A Polymer Physics Perspective</title><source>Wiley-Blackwell Read & Publish Collection</source><creator>Cubuk, Jasmine ; Soranno, Andrea</creator><creatorcontrib>Cubuk, Jasmine ; Soranno, Andrea</creatorcontrib><description>The cell is a crowded environment where a relevant fraction of the available space is occupied by proteins, nucleic acids, and metabolites. Here we discuss recent advancements in the understanding of crowding effects on intrinsically disordered proteins. Differently from their structured counterparts, these proteins do not adopt a stable three‐dimensional structure and remain flexible and dynamic in solution. The physics of polymers and colloids provides a framework to interpret how crowding modulates conformations, dynamics, and interactions of disordered proteins. Flory‐Huggins models enable rationalizing the different degree of compaction induced by crowding agents in terms of depletion interactions. The same interactions modulate the diffusion of the disordered proteins in a crowded milieu and the association and dissociation rates when interacting with a ligand. Altogether, this theoretical framework provides new insights into the interpretation of the effects of the cellular environment on disordered proteins.
The cell is a crowded environment where a relevant fraction of the available space is occupied. Intrinsically disordered proteins do not adopt a stable three‐dimensional structure and therefore are particularly sensitive to such crowded cellular milieu. This Review discusses how the physics of polymers and colloids provides a framework to interpret how crowding modulates conformations and interactions of disordered proteins.</description><identifier>ISSN: 2570-4206</identifier><identifier>EISSN: 2570-4206</identifier><identifier>DOI: 10.1002/syst.202100051</identifier><language>eng</language><publisher>Weinheim: Wiley Subscription Services, Inc</publisher><subject>colloids ; crowding ; intrinsically disordered proteins ; polymers ; proteins</subject><ispartof>ChemSystemsChem, 2022-09, Vol.4 (5), p.n/a</ispartof><rights>2022 Wiley‐VCH GmbH</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3171-4bb5066d61a0974c03d36b03ba048c0c325f7eba7da46ec8a21bedf3ffe4325b3</citedby><cites>FETCH-LOGICAL-c3171-4bb5066d61a0974c03d36b03ba048c0c325f7eba7da46ec8a21bedf3ffe4325b3</cites><orcidid>0000-0001-6915-8242 ; 0000-0001-8394-7993</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Cubuk, Jasmine</creatorcontrib><creatorcontrib>Soranno, Andrea</creatorcontrib><title>Macromolecular Crowding and Intrinsically Disordered Proteins: A Polymer Physics Perspective</title><title>ChemSystemsChem</title><description>The cell is a crowded environment where a relevant fraction of the available space is occupied by proteins, nucleic acids, and metabolites. Here we discuss recent advancements in the understanding of crowding effects on intrinsically disordered proteins. Differently from their structured counterparts, these proteins do not adopt a stable three‐dimensional structure and remain flexible and dynamic in solution. The physics of polymers and colloids provides a framework to interpret how crowding modulates conformations, dynamics, and interactions of disordered proteins. Flory‐Huggins models enable rationalizing the different degree of compaction induced by crowding agents in terms of depletion interactions. The same interactions modulate the diffusion of the disordered proteins in a crowded milieu and the association and dissociation rates when interacting with a ligand. Altogether, this theoretical framework provides new insights into the interpretation of the effects of the cellular environment on disordered proteins.
The cell is a crowded environment where a relevant fraction of the available space is occupied. Intrinsically disordered proteins do not adopt a stable three‐dimensional structure and therefore are particularly sensitive to such crowded cellular milieu. This Review discusses how the physics of polymers and colloids provides a framework to interpret how crowding modulates conformations and interactions of disordered proteins.</description><subject>colloids</subject><subject>crowding</subject><subject>intrinsically disordered proteins</subject><subject>polymers</subject><subject>proteins</subject><issn>2570-4206</issn><issn>2570-4206</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNqFkM1LAzEQxYMoWLRXzwHPrZNkd9N6K_WrUHGh9SAIIZvM6pbtpiZby_73plTUm6eZ4f3eDPMIuWAwZAD8KnShHXLgcYCUHZEeTyUMEg7Z8Z_-lPRDWEWEp0ywseyR10dtvFu7Gs221p5OvdvZqnmjurF01rS-akJldF139KYKzlv0aGnuXYtRuaYTmru6W6On-XsXyUBz9GGDpq0-8ZyclLoO2P-uZ-T57nY5fRjMn-5n08l8YASTbJAURQpZZjOmYSwTA8KKrABRaEhGBozgaSmx0NLqJEMz0pwVaEtRlphErRBn5PKwd-PdxxZDq1Zu65t4UnHJEiY5pDJSwwMVHw7BY6k2vlpr3ykGah-i2oeofkKMhvHBsKtq7P6h1eJlsfz1fgH3cXd7</recordid><startdate>202209</startdate><enddate>202209</enddate><creator>Cubuk, Jasmine</creator><creator>Soranno, Andrea</creator><general>Wiley Subscription Services, Inc</general><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0001-6915-8242</orcidid><orcidid>https://orcid.org/0000-0001-8394-7993</orcidid></search><sort><creationdate>202209</creationdate><title>Macromolecular Crowding and Intrinsically Disordered Proteins: A Polymer Physics Perspective</title><author>Cubuk, Jasmine ; Soranno, Andrea</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3171-4bb5066d61a0974c03d36b03ba048c0c325f7eba7da46ec8a21bedf3ffe4325b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>colloids</topic><topic>crowding</topic><topic>intrinsically disordered proteins</topic><topic>polymers</topic><topic>proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cubuk, Jasmine</creatorcontrib><creatorcontrib>Soranno, Andrea</creatorcontrib><collection>CrossRef</collection><jtitle>ChemSystemsChem</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cubuk, Jasmine</au><au>Soranno, Andrea</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Macromolecular Crowding and Intrinsically Disordered Proteins: A Polymer Physics Perspective</atitle><jtitle>ChemSystemsChem</jtitle><date>2022-09</date><risdate>2022</risdate><volume>4</volume><issue>5</issue><epage>n/a</epage><issn>2570-4206</issn><eissn>2570-4206</eissn><abstract>The cell is a crowded environment where a relevant fraction of the available space is occupied by proteins, nucleic acids, and metabolites. Here we discuss recent advancements in the understanding of crowding effects on intrinsically disordered proteins. Differently from their structured counterparts, these proteins do not adopt a stable three‐dimensional structure and remain flexible and dynamic in solution. The physics of polymers and colloids provides a framework to interpret how crowding modulates conformations, dynamics, and interactions of disordered proteins. Flory‐Huggins models enable rationalizing the different degree of compaction induced by crowding agents in terms of depletion interactions. The same interactions modulate the diffusion of the disordered proteins in a crowded milieu and the association and dissociation rates when interacting with a ligand. Altogether, this theoretical framework provides new insights into the interpretation of the effects of the cellular environment on disordered proteins.
The cell is a crowded environment where a relevant fraction of the available space is occupied. Intrinsically disordered proteins do not adopt a stable three‐dimensional structure and therefore are particularly sensitive to such crowded cellular milieu. This Review discusses how the physics of polymers and colloids provides a framework to interpret how crowding modulates conformations and interactions of disordered proteins.</abstract><cop>Weinheim</cop><pub>Wiley Subscription Services, Inc</pub><doi>10.1002/syst.202100051</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0001-6915-8242</orcidid><orcidid>https://orcid.org/0000-0001-8394-7993</orcidid></addata></record> |
fulltext | fulltext |
identifier | ISSN: 2570-4206 |
ispartof | ChemSystemsChem, 2022-09, Vol.4 (5), p.n/a |
issn | 2570-4206 2570-4206 |
language | eng |
recordid | cdi_proquest_journals_2714172057 |
source | Wiley-Blackwell Read & Publish Collection |
subjects | colloids crowding intrinsically disordered proteins polymers proteins |
title | Macromolecular Crowding and Intrinsically Disordered Proteins: A Polymer Physics Perspective |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T04%3A57%3A56IST&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=Macromolecular%20Crowding%20and%20Intrinsically%20Disordered%20Proteins:%20A%20Polymer%20Physics%20Perspective&rft.jtitle=ChemSystemsChem&rft.au=Cubuk,%20Jasmine&rft.date=2022-09&rft.volume=4&rft.issue=5&rft.epage=n/a&rft.issn=2570-4206&rft.eissn=2570-4206&rft_id=info:doi/10.1002/syst.202100051&rft_dat=%3Cproquest_cross%3E2714172057%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c3171-4bb5066d61a0974c03d36b03ba048c0c325f7eba7da46ec8a21bedf3ffe4325b3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2714172057&rft_id=info:pmid/&rfr_iscdi=true |