Network model of a protein globule

Phase transition of a protein globule is considered in the frameworks of (i) the generalized mean-field theory for the order parameter, characterizing the extent of the deviation of a protein three-dimensional structure from its native state and (ii) the network model that treats a protein globule a...

Full description

Saved in:
Bibliographic Details
Published in:Journal of biological physics 2013-09, Vol.39 (4), p.673-685
Main Authors: Meilikhov, E. Z., Farzetdinova, R. M.
Format: Article
Language:English
Subjects:
Amino acids
Biochemistry
Biological and Medical Physics
Biophysics
Complex Fluids and Microfluidics
Complex Systems
Models, Molecular
Neurosciences
Original Paper
Phase transitions
Physics
Physics and Astronomy
Polypeptides
Protein Stability
Proteins
Proteins - chemistry
Soft and Granular Matter
Temperature
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-c470t-81e71cdccb663b61fa8578cdd07794fd909871edcba2a987da9c6780e0b6f7843
cites cdi_FETCH-LOGICAL-c470t-81e71cdccb663b61fa8578cdd07794fd909871edcba2a987da9c6780e0b6f7843
container_end_page 685
container_issue 4
container_start_page 673
container_title Journal of biological physics
container_volume 39
creator Meilikhov, E. Z.
Farzetdinova, R. M.
description Phase transition of a protein globule is considered in the frameworks of (i) the generalized mean-field theory for the order parameter, characterizing the extent of the deviation of a protein three-dimensional structure from its native state and (ii) the network model that treats a protein globule as a small-world network with a significant percent of long-range links between amino acid residues. Temperature dependencies of the introduced order parameter are defined and phase-transition temperatures are found on the basis of the function defining the distribution of links’ numbers for protein residues. An important role of long-range links, promoting considerable rise of thermal protein stability, is demonstrated by the example of a correlation between protein melting temperature and a fraction of disulfide bonds.
doi_str_mv 10.1007/s10867-013-9326-8
format article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3758824</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3077277911</sourcerecordid><originalsourceid>FETCH-LOGICAL-c470t-81e71cdccb663b61fa8578cdd07794fd909871edcba2a987da9c6780e0b6f7843</originalsourceid><addsrcrecordid>eNp1kU1LxDAQhoMo7rr6A7xI0YuX6iRt83ERZPELFr3oOaRpunZtmzVpFf-9Wbouq-AhZIZ55p1MXoSOMVxgAHbpMXDKYsBJLBJCY76DxjhjSQyUi100BhAkxEBH6MD7BYSck2wfjUjCBQOajtHpo-k-rXuLGluYOrJlpKKls52p2mhe27yvzSHaK1XtzdH6nqCX25vn6X08e7p7mF7PYp0y6GKODcO60DqnNMkpLhXPGNdFAYyJtCxEGM6wKXSuiAphoYSmjIOBnJaMp8kEXQ26yz5vAmfazqlaLl3VKPclrark70pbvcq5_ZAJyzgnK4HztYCz773xnWwqr01dq9bY3kucEkHD4VlAz_6gC9u7NqwXqCTFBAjFgcIDpZ313ply8xgMcuWAHByQwQG5ckDy0HOyvcWm4-fLA0AGwIdSOzdua_S_qt-wtJAh</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1434120261</pqid></control><display><type>article</type><title>Network model of a protein globule</title><source>Springer Nature</source><source>PubMed Central</source><creator>Meilikhov, E. Z. ; Farzetdinova, R. M.</creator><creatorcontrib>Meilikhov, E. Z. ; Farzetdinova, R. M.</creatorcontrib><description>Phase transition of a protein globule is considered in the frameworks of (i) the generalized mean-field theory for the order parameter, characterizing the extent of the deviation of a protein three-dimensional structure from its native state and (ii) the network model that treats a protein globule as a small-world network with a significant percent of long-range links between amino acid residues. Temperature dependencies of the introduced order parameter are defined and phase-transition temperatures are found on the basis of the function defining the distribution of links’ numbers for protein residues. An important role of long-range links, promoting considerable rise of thermal protein stability, is demonstrated by the example of a correlation between protein melting temperature and a fraction of disulfide bonds.</description><identifier>ISSN: 0092-0606</identifier><identifier>EISSN: 1573-0689</identifier><identifier>DOI: 10.1007/s10867-013-9326-8</identifier><identifier>PMID: 23897064</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Amino acids ; Biochemistry ; Biological and Medical Physics ; Biophysics ; Complex Fluids and Microfluidics ; Complex Systems ; Models, Molecular ; Neurosciences ; Original Paper ; Phase transitions ; Physics ; Physics and Astronomy ; Polypeptides ; Protein Stability ; Proteins ; Proteins - chemistry ; Soft and Granular Matter ; Temperature</subject><ispartof>Journal of biological physics, 2013-09, Vol.39 (4), p.673-685</ispartof><rights>Springer Science+Business Media Dordrecht 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-81e71cdccb663b61fa8578cdd07794fd909871edcba2a987da9c6780e0b6f7843</citedby><cites>FETCH-LOGICAL-c470t-81e71cdccb663b61fa8578cdd07794fd909871edcba2a987da9c6780e0b6f7843</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3758824/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3758824/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23897064$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Meilikhov, E. Z.</creatorcontrib><creatorcontrib>Farzetdinova, R. M.</creatorcontrib><title>Network model of a protein globule</title><title>Journal of biological physics</title><addtitle>J Biol Phys</addtitle><addtitle>J Biol Phys</addtitle><description>Phase transition of a protein globule is considered in the frameworks of (i) the generalized mean-field theory for the order parameter, characterizing the extent of the deviation of a protein three-dimensional structure from its native state and (ii) the network model that treats a protein globule as a small-world network with a significant percent of long-range links between amino acid residues. Temperature dependencies of the introduced order parameter are defined and phase-transition temperatures are found on the basis of the function defining the distribution of links’ numbers for protein residues. An important role of long-range links, promoting considerable rise of thermal protein stability, is demonstrated by the example of a correlation between protein melting temperature and a fraction of disulfide bonds.</description><subject>Amino acids</subject><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biophysics</subject><subject>Complex Fluids and Microfluidics</subject><subject>Complex Systems</subject><subject>Models, Molecular</subject><subject>Neurosciences</subject><subject>Original Paper</subject><subject>Phase transitions</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Polypeptides</subject><subject>Protein Stability</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Soft and Granular Matter</subject><subject>Temperature</subject><issn>0092-0606</issn><issn>1573-0689</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNp1kU1LxDAQhoMo7rr6A7xI0YuX6iRt83ERZPELFr3oOaRpunZtmzVpFf-9Wbouq-AhZIZ55p1MXoSOMVxgAHbpMXDKYsBJLBJCY76DxjhjSQyUi100BhAkxEBH6MD7BYSck2wfjUjCBQOajtHpo-k-rXuLGluYOrJlpKKls52p2mhe27yvzSHaK1XtzdH6nqCX25vn6X08e7p7mF7PYp0y6GKODcO60DqnNMkpLhXPGNdFAYyJtCxEGM6wKXSuiAphoYSmjIOBnJaMp8kEXQ26yz5vAmfazqlaLl3VKPclrark70pbvcq5_ZAJyzgnK4HztYCz773xnWwqr01dq9bY3kucEkHD4VlAz_6gC9u7NqwXqCTFBAjFgcIDpZ313ply8xgMcuWAHByQwQG5ckDy0HOyvcWm4-fLA0AGwIdSOzdua_S_qt-wtJAh</recordid><startdate>20130901</startdate><enddate>20130901</enddate><creator>Meilikhov, E. Z.</creator><creator>Farzetdinova, R. M.</creator><general>Springer Netherlands</general><general>Springer Nature B.V</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>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20130901</creationdate><title>Network model of a protein globule</title><author>Meilikhov, E. Z. ; Farzetdinova, R. M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c470t-81e71cdccb663b61fa8578cdd07794fd909871edcba2a987da9c6780e0b6f7843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino acids</topic><topic>Biochemistry</topic><topic>Biological and Medical Physics</topic><topic>Biophysics</topic><topic>Complex Fluids and Microfluidics</topic><topic>Complex Systems</topic><topic>Models, Molecular</topic><topic>Neurosciences</topic><topic>Original Paper</topic><topic>Phase transitions</topic><topic>Physics</topic><topic>Physics and Astronomy</topic><topic>Polypeptides</topic><topic>Protein Stability</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Soft and Granular Matter</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meilikhov, E. Z.</creatorcontrib><creatorcontrib>Farzetdinova, R. M.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Research Library China</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of biological physics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Meilikhov, E. Z.</au><au>Farzetdinova, R. M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Network model of a protein globule</atitle><jtitle>Journal of biological physics</jtitle><stitle>J Biol Phys</stitle><addtitle>J Biol Phys</addtitle><date>2013-09-01</date><risdate>2013</risdate><volume>39</volume><issue>4</issue><spage>673</spage><epage>685</epage><pages>673-685</pages><issn>0092-0606</issn><eissn>1573-0689</eissn><abstract>Phase transition of a protein globule is considered in the frameworks of (i) the generalized mean-field theory for the order parameter, characterizing the extent of the deviation of a protein three-dimensional structure from its native state and (ii) the network model that treats a protein globule as a small-world network with a significant percent of long-range links between amino acid residues. Temperature dependencies of the introduced order parameter are defined and phase-transition temperatures are found on the basis of the function defining the distribution of links’ numbers for protein residues. An important role of long-range links, promoting considerable rise of thermal protein stability, is demonstrated by the example of a correlation between protein melting temperature and a fraction of disulfide bonds.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>23897064</pmid><doi>10.1007/s10867-013-9326-8</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0092-0606
ispartof Journal of biological physics, 2013-09, Vol.39 (4), p.673-685
issn 0092-0606
1573-0689
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3758824
source Springer Nature; PubMed Central
subjects Amino acids
Biochemistry
Biological and Medical Physics
Biophysics
Complex Fluids and Microfluidics
Complex Systems
Models, Molecular
Neurosciences
Original Paper
Phase transitions
Physics
Physics and Astronomy
Polypeptides
Protein Stability
Proteins
Proteins - chemistry
Soft and Granular Matter
Temperature
title Network model of a protein globule
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-29T23%3A58%3A42IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Network%20model%20of%20a%20protein%20globule&rft.jtitle=Journal%20of%20biological%20physics&rft.au=Meilikhov,%20E.%20Z.&rft.date=2013-09-01&rft.volume=39&rft.issue=4&rft.spage=673&rft.epage=685&rft.pages=673-685&rft.issn=0092-0606&rft.eissn=1573-0689&rft_id=info:doi/10.1007/s10867-013-9326-8&rft_dat=%3Cproquest_pubme%3E3077277911%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c470t-81e71cdccb663b61fa8578cdd07794fd909871edcba2a987da9c6780e0b6f7843%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1434120261&rft_id=info:pmid/23897064&rfr_iscdi=true