Loading…
Configurational entropy of native proteins
Simulations of the residual configurational entropy of a protein in the native state suggest that it is nearly an order of magnitude larger than the entropy of denaturation. The implications of this result are discussed.
Saved in:
Published in: | Biophysical journal 1987-12, Vol.52 (6), p.1083-1085 |
---|---|
Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | 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-c491t-f14f58e99bb9ebfe6c751080e273ef3960a4e3adf092baa52e7db363b2e1af6a3 |
---|---|
cites | |
container_end_page | 1085 |
container_issue | 6 |
container_start_page | 1083 |
container_title | Biophysical journal |
container_volume | 52 |
creator | Karplus, M. Ichiye, T. Pettitt, B.M. |
description | Simulations of the residual configurational entropy of a protein in the native state suggest that it is nearly an order of magnitude larger than the entropy of denaturation. The implications of this result are discussed. |
doi_str_mv | 10.1016/S0006-3495(87)83303-9 |
format | article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1330109</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006349587833039</els_id><sourcerecordid>77897724</sourcerecordid><originalsourceid>FETCH-LOGICAL-c491t-f14f58e99bb9ebfe6c751080e273ef3960a4e3adf092baa52e7db363b2e1af6a3</originalsourceid><addsrcrecordid>eNqFkE1LAzEQhoMotVZ_QqEHERVWJ5vdzeaiSPELCh7Uc8hmJxrZJjXZFvrv3X5Q9OQpkHnmnZeHkCGFKwq0uH4FgCJhmcjPS35RMgYsEXukT_MsTQDKYp_0d8ghOYrxC4CmOdAe6bEs5VTwPrkce2fsxzyo1nqnmhG6NvjZcuTNyHV_CxzNgm_RunhMDoxqIp5s3wF5f7h_Gz8lk5fH5_HdJNGZoG1iaGbyEoWoKoGVwULznEIJmHKGhokCVIZM1QZEWimVp8jrihWsSpEqUyg2IDeb3Nm8mmKtV41UI2fBTlVYSq-s_Dtx9lN--IWknQMKogs42wYE_z3H2MqpjRqbRjn08yg5LwXnadaB-QbUwccY0OyOUJAryXItWa4MypLLtWS5OjD83XC3tbXazU-3cxW1akxQTtu4wzjPeNehw243GHY2FxaDjNqi01jbgLqVtbf_FPkBp3maRA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>77897724</pqid></control><display><type>article</type><title>Configurational entropy of native proteins</title><source>Open Access: PubMed Central</source><creator>Karplus, M. ; Ichiye, T. ; Pettitt, B.M.</creator><creatorcontrib>Karplus, M. ; Ichiye, T. ; Pettitt, B.M.</creatorcontrib><description>Simulations of the residual configurational entropy of a protein in the native state suggest that it is nearly an order of magnitude larger than the entropy of denaturation. The implications of this result are discussed.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(87)83303-9</identifier><identifier>PMID: 3427197</identifier><identifier>CODEN: BIOJAU</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Mathematics ; Molecular biophysics ; Protein Conformation ; Proteins ; Structure in molecular biology ; Thermodynamics ; Tridimensional structure</subject><ispartof>Biophysical journal, 1987-12, Vol.52 (6), p.1083-1085</ispartof><rights>1987 The Biophysical Society</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c491t-f14f58e99bb9ebfe6c751080e273ef3960a4e3adf092baa52e7db363b2e1af6a3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1330109/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1330109/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7747778$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3427197$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Karplus, M.</creatorcontrib><creatorcontrib>Ichiye, T.</creatorcontrib><creatorcontrib>Pettitt, B.M.</creatorcontrib><title>Configurational entropy of native proteins</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>Simulations of the residual configurational entropy of a protein in the native state suggest that it is nearly an order of magnitude larger than the entropy of denaturation. The implications of this result are discussed.</description><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Mathematics</subject><subject>Molecular biophysics</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Structure in molecular biology</subject><subject>Thermodynamics</subject><subject>Tridimensional structure</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><recordid>eNqFkE1LAzEQhoMotVZ_QqEHERVWJ5vdzeaiSPELCh7Uc8hmJxrZJjXZFvrv3X5Q9OQpkHnmnZeHkCGFKwq0uH4FgCJhmcjPS35RMgYsEXukT_MsTQDKYp_0d8ghOYrxC4CmOdAe6bEs5VTwPrkce2fsxzyo1nqnmhG6NvjZcuTNyHV_CxzNgm_RunhMDoxqIp5s3wF5f7h_Gz8lk5fH5_HdJNGZoG1iaGbyEoWoKoGVwULznEIJmHKGhokCVIZM1QZEWimVp8jrihWsSpEqUyg2IDeb3Nm8mmKtV41UI2fBTlVYSq-s_Dtx9lN--IWknQMKogs42wYE_z3H2MqpjRqbRjn08yg5LwXnadaB-QbUwccY0OyOUJAryXItWa4MypLLtWS5OjD83XC3tbXazU-3cxW1akxQTtu4wzjPeNehw243GHY2FxaDjNqi01jbgLqVtbf_FPkBp3maRA</recordid><startdate>19871201</startdate><enddate>19871201</enddate><creator>Karplus, M.</creator><creator>Ichiye, T.</creator><creator>Pettitt, B.M.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>19871201</creationdate><title>Configurational entropy of native proteins</title><author>Karplus, M. ; Ichiye, T. ; Pettitt, B.M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c491t-f14f58e99bb9ebfe6c751080e273ef3960a4e3adf092baa52e7db363b2e1af6a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Mathematics</topic><topic>Molecular biophysics</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Structure in molecular biology</topic><topic>Thermodynamics</topic><topic>Tridimensional structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Karplus, M.</creatorcontrib><creatorcontrib>Ichiye, T.</creatorcontrib><creatorcontrib>Pettitt, B.M.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</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>Karplus, M.</au><au>Ichiye, T.</au><au>Pettitt, B.M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Configurational entropy of native proteins</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1987-12-01</date><risdate>1987</risdate><volume>52</volume><issue>6</issue><spage>1083</spage><epage>1085</epage><pages>1083-1085</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><coden>BIOJAU</coden><abstract>Simulations of the residual configurational entropy of a protein in the native state suggest that it is nearly an order of magnitude larger than the entropy of denaturation. The implications of this result are discussed.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3427197</pmid><doi>10.1016/S0006-3495(87)83303-9</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0006-3495 |
ispartof | Biophysical journal, 1987-12, Vol.52 (6), p.1083-1085 |
issn | 0006-3495 1542-0086 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1330109 |
source | Open Access: PubMed Central |
subjects | Biological and medical sciences Fundamental and applied biological sciences. Psychology Mathematics Molecular biophysics Protein Conformation Proteins Structure in molecular biology Thermodynamics Tridimensional structure |
title | Configurational entropy of native proteins |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T09%3A08%3A21IST&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=Configurational%20entropy%20of%20native%20proteins&rft.jtitle=Biophysical%20journal&rft.au=Karplus,%20M.&rft.date=1987-12-01&rft.volume=52&rft.issue=6&rft.spage=1083&rft.epage=1085&rft.pages=1083-1085&rft.issn=0006-3495&rft.eissn=1542-0086&rft.coden=BIOJAU&rft_id=info:doi/10.1016/S0006-3495(87)83303-9&rft_dat=%3Cproquest_pubme%3E77897724%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c491t-f14f58e99bb9ebfe6c751080e273ef3960a4e3adf092baa52e7db363b2e1af6a3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=77897724&rft_id=info:pmid/3427197&rfr_iscdi=true |