Loading…

New insights into disordered proteins and regions according to the FOD-M model

A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit (chain / domain). The analysis includes all the...

Full description

Saved in:
Bibliographic Details
Published in:PloS one 2022-10, Vol.17 (10), p.e0275300
Main Authors: Roterman, Irena, Stapor, Katarzyna, Fabian, Piotr, Konieczny, Leszek
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-c692t-46377f91882c34497d485f11cb88ed0c195732de6ca0d6c5c6f6b32cd7bf723c3
cites cdi_FETCH-LOGICAL-c692t-46377f91882c34497d485f11cb88ed0c195732de6ca0d6c5c6f6b32cd7bf723c3
container_end_page
container_issue 10
container_start_page e0275300
container_title PloS one
container_volume 17
creator Roterman, Irena
Stapor, Katarzyna
Fabian, Piotr
Konieczny, Leszek
description A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit (chain / domain). The analysis includes all the Homo Sapiens as well as Mus Musculus proteins present in the DisProt database for which the structure is available. In the analysis, the fuzzy oil drop modified model (FOD-M) was used, taking into account the external force field, modified by the presence of other factors apart from polar water, influencing protein structuring. The paper presents an alternative to secondary-structure-based classification of intrinsically disordered regions (IDR). The basis of our classification is the ordering of hydrophobic core as calculated by the FOD-M model resulting in FOD-ordered or FOD-unordered IDRs.
doi_str_mv 10.1371/journal.pone.0275300
format article
fullrecord <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_2723465767</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A721780981</galeid><doaj_id>oai_doaj_org_article_e380e3a8f5324af5a9d1ce2284b8b2ac</doaj_id><sourcerecordid>A721780981</sourcerecordid><originalsourceid>FETCH-LOGICAL-c692t-46377f91882c34497d485f11cb88ed0c195732de6ca0d6c5c6f6b32cd7bf723c3</originalsourceid><addsrcrecordid>eNqNkttu1DAQhiMEoqXwBggiISG42MWHxHZukKpCYaXSlTjdWo49ybrKxlvb4fD2OGxabVAvkC888nzzjz3-s-wpRktMOX5z5Qbfq265cz0sEeElRehedowrShaMIHr_ID7KHoVwhVBJBWMPsyPKCC5JWRxnl5fwM7d9sO0mhhRElxsbnDfgweQ77yKkbK56k3torRtjrVPe9m2e4LiB_Hz9bvEp3zoD3ePsQaO6AE-m_ST7dv7-69nHxcX6w-rs9GKhWUXiomCU86bCQhBNi6LiphBlg7GuhQCDNK5KTokBphUyTJeaNaymRBteN5xQTU-y53vdXeeCnEYRJEnJgpWc8USs9oRx6kruvN0q_1s6ZeXfA-dbqXy0ugMJVCCgSjQlJYVqSlUZrIEQUdSiJmrs9nbqNtRbMBr66FU3E51neruRrfshq7JESBRJ4NUk4N31ACHKrQ0auk714Ibp3qIQDCX0xT_o3a-bqFalB9i-camvHkXlKSeYC1QJnKjlHVRaBrZWJ980Np3PCl7PChIT4Vds1RCCXH35_P_s-vucfXnAbkB1cRNcN8TRUHOw2IPauxA8NLdDxkiOtr-ZhhxtLyfbp7Jnhx90W3Tjc_oHxjj71g</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2723465767</pqid></control><display><type>article</type><title>New insights into disordered proteins and regions according to the FOD-M model</title><source>ProQuest - Publicly Available Content Database</source><source>PubMed Central</source><creator>Roterman, Irena ; Stapor, Katarzyna ; Fabian, Piotr ; Konieczny, Leszek</creator><contributor>Sussman, Joel L.</contributor><creatorcontrib>Roterman, Irena ; Stapor, Katarzyna ; Fabian, Piotr ; Konieczny, Leszek ; Sussman, Joel L.</creatorcontrib><description>A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit (chain / domain). The analysis includes all the Homo Sapiens as well as Mus Musculus proteins present in the DisProt database for which the structure is available. In the analysis, the fuzzy oil drop modified model (FOD-M) was used, taking into account the external force field, modified by the presence of other factors apart from polar water, influencing protein structuring. The paper presents an alternative to secondary-structure-based classification of intrinsically disordered regions (IDR). The basis of our classification is the ordering of hydrophobic core as calculated by the FOD-M model resulting in FOD-ordered or FOD-unordered IDRs.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0275300</identifier><identifier>PMID: 36215254</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Analysis ; Animal models in research ; Animals ; Biology and Life Sciences ; Classification ; Evaluation ; Humans ; Hydrophobic and Hydrophilic Interactions ; Hydrophobicity ; Intrinsically Disordered Proteins - chemistry ; Mice ; Polar waters ; Protein Conformation ; Protein Structure, Secondary ; Proteins ; Research and Analysis Methods ; Water</subject><ispartof>PloS one, 2022-10, Vol.17 (10), p.e0275300</ispartof><rights>COPYRIGHT 2022 Public Library of Science</rights><rights>2022 Roterman et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 Roterman et al 2022 Roterman et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-46377f91882c34497d485f11cb88ed0c195732de6ca0d6c5c6f6b32cd7bf723c3</citedby><cites>FETCH-LOGICAL-c692t-46377f91882c34497d485f11cb88ed0c195732de6ca0d6c5c6f6b32cd7bf723c3</cites><orcidid>0000-0003-3003-6592 ; 0000-0002-5152-6331 ; 0000-0003-3652-9099</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2723465767/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2723465767?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36215254$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Sussman, Joel L.</contributor><creatorcontrib>Roterman, Irena</creatorcontrib><creatorcontrib>Stapor, Katarzyna</creatorcontrib><creatorcontrib>Fabian, Piotr</creatorcontrib><creatorcontrib>Konieczny, Leszek</creatorcontrib><title>New insights into disordered proteins and regions according to the FOD-M model</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit (chain / domain). The analysis includes all the Homo Sapiens as well as Mus Musculus proteins present in the DisProt database for which the structure is available. In the analysis, the fuzzy oil drop modified model (FOD-M) was used, taking into account the external force field, modified by the presence of other factors apart from polar water, influencing protein structuring. The paper presents an alternative to secondary-structure-based classification of intrinsically disordered regions (IDR). The basis of our classification is the ordering of hydrophobic core as calculated by the FOD-M model resulting in FOD-ordered or FOD-unordered IDRs.</description><subject>Analysis</subject><subject>Animal models in research</subject><subject>Animals</subject><subject>Biology and Life Sciences</subject><subject>Classification</subject><subject>Evaluation</subject><subject>Humans</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Hydrophobicity</subject><subject>Intrinsically Disordered Proteins - chemistry</subject><subject>Mice</subject><subject>Polar waters</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Research and Analysis Methods</subject><subject>Water</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNqNkttu1DAQhiMEoqXwBggiISG42MWHxHZukKpCYaXSlTjdWo49ybrKxlvb4fD2OGxabVAvkC888nzzjz3-s-wpRktMOX5z5Qbfq265cz0sEeElRehedowrShaMIHr_ID7KHoVwhVBJBWMPsyPKCC5JWRxnl5fwM7d9sO0mhhRElxsbnDfgweQ77yKkbK56k3torRtjrVPe9m2e4LiB_Hz9bvEp3zoD3ePsQaO6AE-m_ST7dv7-69nHxcX6w-rs9GKhWUXiomCU86bCQhBNi6LiphBlg7GuhQCDNK5KTokBphUyTJeaNaymRBteN5xQTU-y53vdXeeCnEYRJEnJgpWc8USs9oRx6kruvN0q_1s6ZeXfA-dbqXy0ugMJVCCgSjQlJYVqSlUZrIEQUdSiJmrs9nbqNtRbMBr66FU3E51neruRrfshq7JESBRJ4NUk4N31ACHKrQ0auk714Ibp3qIQDCX0xT_o3a-bqFalB9i-camvHkXlKSeYC1QJnKjlHVRaBrZWJ980Np3PCl7PChIT4Vds1RCCXH35_P_s-vucfXnAbkB1cRNcN8TRUHOw2IPauxA8NLdDxkiOtr-ZhhxtLyfbp7Jnhx90W3Tjc_oHxjj71g</recordid><startdate>20221010</startdate><enddate>20221010</enddate><creator>Roterman, Irena</creator><creator>Stapor, Katarzyna</creator><creator>Fabian, Piotr</creator><creator>Konieczny, Leszek</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0003-3003-6592</orcidid><orcidid>https://orcid.org/0000-0002-5152-6331</orcidid><orcidid>https://orcid.org/0000-0003-3652-9099</orcidid></search><sort><creationdate>20221010</creationdate><title>New insights into disordered proteins and regions according to the FOD-M model</title><author>Roterman, Irena ; Stapor, Katarzyna ; Fabian, Piotr ; Konieczny, Leszek</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-46377f91882c34497d485f11cb88ed0c195732de6ca0d6c5c6f6b32cd7bf723c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Analysis</topic><topic>Animal models in research</topic><topic>Animals</topic><topic>Biology and Life Sciences</topic><topic>Classification</topic><topic>Evaluation</topic><topic>Humans</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Hydrophobicity</topic><topic>Intrinsically Disordered Proteins - chemistry</topic><topic>Mice</topic><topic>Polar waters</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Research and Analysis Methods</topic><topic>Water</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Roterman, Irena</creatorcontrib><creatorcontrib>Stapor, Katarzyna</creatorcontrib><creatorcontrib>Fabian, Piotr</creatorcontrib><creatorcontrib>Konieczny, Leszek</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing &amp; Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological &amp; Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science &amp; Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>Advanced Technologies &amp; Aerospace Collection</collection><collection>Agricultural &amp; Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing &amp; Allied Health Database (Alumni Edition)</collection><collection>Meteorological &amp; Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agriculture Science Database</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Engineering Database</collection><collection>Nursing &amp; Allied Health Premium</collection><collection>ProQuest advanced technologies &amp; aerospace journals</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials science collection</collection><collection>ProQuest - Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Roterman, Irena</au><au>Stapor, Katarzyna</au><au>Fabian, Piotr</au><au>Konieczny, Leszek</au><au>Sussman, Joel L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>New insights into disordered proteins and regions according to the FOD-M model</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2022-10-10</date><risdate>2022</risdate><volume>17</volume><issue>10</issue><spage>e0275300</spage><pages>e0275300-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit (chain / domain). The analysis includes all the Homo Sapiens as well as Mus Musculus proteins present in the DisProt database for which the structure is available. In the analysis, the fuzzy oil drop modified model (FOD-M) was used, taking into account the external force field, modified by the presence of other factors apart from polar water, influencing protein structuring. The paper presents an alternative to secondary-structure-based classification of intrinsically disordered regions (IDR). The basis of our classification is the ordering of hydrophobic core as calculated by the FOD-M model resulting in FOD-ordered or FOD-unordered IDRs.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>36215254</pmid><doi>10.1371/journal.pone.0275300</doi><orcidid>https://orcid.org/0000-0003-3003-6592</orcidid><orcidid>https://orcid.org/0000-0002-5152-6331</orcidid><orcidid>https://orcid.org/0000-0003-3652-9099</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1932-6203
ispartof PloS one, 2022-10, Vol.17 (10), p.e0275300
issn 1932-6203
1932-6203
language eng
recordid cdi_plos_journals_2723465767
source ProQuest - Publicly Available Content Database; PubMed Central
subjects Analysis
Animal models in research
Animals
Biology and Life Sciences
Classification
Evaluation
Humans
Hydrophobic and Hydrophilic Interactions
Hydrophobicity
Intrinsically Disordered Proteins - chemistry
Mice
Polar waters
Protein Conformation
Protein Structure, Secondary
Proteins
Research and Analysis Methods
Water
title New insights into disordered proteins and regions according to the FOD-M model
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T08%3A41%3A29IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=New%20insights%20into%20disordered%20proteins%20and%20regions%20according%20to%20the%20FOD-M%20model&rft.jtitle=PloS%20one&rft.au=Roterman,%20Irena&rft.date=2022-10-10&rft.volume=17&rft.issue=10&rft.spage=e0275300&rft.pages=e0275300-&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0275300&rft_dat=%3Cgale_plos_%3EA721780981%3C/gale_plos_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c692t-46377f91882c34497d485f11cb88ed0c195732de6ca0d6c5c6f6b32cd7bf723c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2723465767&rft_id=info:pmid/36215254&rft_galeid=A721780981&rfr_iscdi=true