https://m2.mtmt.hu/ hun 2026-10-24 07:38 JournalArticle 32552670 APPROVED true Institute of Enzymology, Research Centre for Natural Sciences, Eötvös Loránd Research Network, Budapest, 1117, Hungary Department of Physiology, Faculty of Medicine, Semmelweis University, Budapest, 1094, Hungary Export Date: 29 December 2021 Correspondence Address: Simon, I.; Institute of Enzymology, Hungary; email: simon.istvan@ttk.hu 0 false 2026-10-22T00:45:24.057+0000 2025-07-01T19:19:15.831+0000 2021-12-29T08:10:33.936+0000 true 10080205 Szalóky-Siki Ágnes /api/admin/10080205 Admin true 2026-04-09T07:37:21.563+0000 true false true 24 24 /api/publicationtype/24 PublicationType 1 true 24 JournalArticle true 10000059 Article true 24 24 /api/publicationtype/24 PublicationType 1 true 24 JournalArticle /api/subtype/10000059 Szakcikk SubType 101 true 10000059 true 1 /api/category/1 Category true 1 Magyar, C. Origin of increased solvent accessibility of peptide bonds in mutual synergetic folding proteins true true /api/journal/10003252 REVIEWED true false 10003252 false 10003252 true 1661-6596 1422-0067 Journal FOREIGN 22 24 13404 13404 10 2021 Mutual Synergetic Folding (MSF) proteins belong to a recently discovered class of proteins. These proteins are disordered in their monomeric but ordered in their oligomeric forms. Their amino acid composition is more similar to globular proteins than to disordered ones. Our preceding work shed light on important structural aspects of the structural organization of these proteins, but the background of this behavior is still unknown. We suggest that solvent accessibility is an important factor, especially solvent accessibility of the peptide bonds can be accounted for this phenomenon. The side chains of the amino acids which form a peptide bond have a high local contribution to the shielding of the peptide bond from the solvent. During the oligomerization step, other non-local residues contribute to the shielding. We investigated these local and non-local effects of shielding based on Shannon information entropy calculations. We found that MSF and globular homodimeric proteins have different local contributions resulting from different amino acid pair frequencies. Their non-local distribution is also different because of distinctive inter-subunit contacts. 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(<span class="authorship-author-name">Magyar Csaba</span> <span class="authorAux-mtmt"> Fehérjék szerkezeti stabilitása, szerkezet alap...</span>) </a> </span> <span class="author-affil"><span title="Természettudományi Kutatóközpont">TTK</span>/Enzimológiai Intézet</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10044957"><a href="/gui2/?type=authors&mode=browse&sel=10044957" target="_blank">Mentes A.<sup>*</sup> (<span class="authorship-author-name">Mentes Anikó</span> <span class="authorAux-mtmt"> Mikrobiális ökológia, bioinformatika</span>) </a> </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10015497"><a href="/gui2/?type=authors&mode=browse&sel=10015497" target="_blank">Cserző M. (<span class="authorship-author-name">Cserző Miklós</span> <span class="authorAux-mtmt"> Fehérjék molekuláris modellezése</span>) </a> </span> <span class="author-affil"><span title="Természettudományi Kutatóközpont">TTK</span>/Enzimológiai Intézet; <span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Élettani Intézet</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10000249"><a href="/gui2/?type=authors&mode=browse&sel=10000249" target="_blank">Simon I. ✉ (<span class="authorship-author-name">Simon István</span> <span class="authorAux-mtmt"> biofizika, biokémia, bioinformatika</span>) </a> </span> <span class="author-affil"><span title="Természettudományi Kutatóközpont">TTK</span>/Enzimológiai Intézet</span> </div> </div> <div class="title"><a href="/gui2/?mode=browse&params=publication;32552670" target="_blank">Origin of increased solvent accessibility of peptide bonds in mutual synergetic folding proteins</a></div> <div> <span class="journal-title">INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES</span> <span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/1661-6596">1661-6596</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1422-0067">1422-0067</a>)</span>: <span class="journal-volume">22</span> <span class="journal-issue">24</span> <span class="page"> Paper 13404. 10 p. </span> <span class="year">(2021)</span> </div> <div class="pub-footer"> <span class="language" xmlns="http://www.w3.org/1999/html">Nyelv: Angol | </span> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.3390/ijms222413404" target="_blank" href="https://doi.org/10.3390/ijms222413404"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000738547900001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000738547900001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85121364423" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85121364423"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="34948202" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=34948202&dopt=Abstract"> PubMed </a> </span> </span> <OnlyViewableByAuthor><div class="ratings"> <div class="journal-subject">Folyóirat szakterülete: Scopus - Spectroscopy&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;D1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Computer Science Applications&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Inorganic Chemistry&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Medicine (miscellaneous)&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Organic Chemistry&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Physical and Theoretical Chemistry&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Catalysis&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q2</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Molecular Biology&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q2</div> </div></OnlyViewableByAuthor> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 4</span> | Független: 2 | Függő: 2 | Nem jelölt: 0 | WoS jelölt: 4 | Scopus jelölt:&nbsp;2 | WoS/Scopus jelölt:&nbsp;4 | DOI jelölt:&nbsp;4 </div> <div class="publication-citation"> <a target="_blank" href="/api/publication?cond=citations.related;eq;32552670&sort=publishedYear,desc&sort=title"> Idézett közlemények száma: 6 </a> </div> <div class="mtid"><span class="long-pub-mtid">Közlemény: 32552670</span> | <span class="status-data status-APPROVED"> Nyilvános </span> Forrás Idéző | <span class="type-subtype">Folyóiratcikk ( Szakcikk ) </span> | <span class="pub-category">Tudományos</span> | <span class="publication-sourceOfData">Scopus</span> </div> <div class="special-affiliations"> Speciális affiliáció: Akadémikus bibliográfia </div> <div class="funder"> (K115698) </div> <div class="lastModified">Utolsó módosítás: 2025.07.01. 21:19 Ladányi Gusztáv (MTMT API user, admin) </div> <pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Institute of Enzymology, Research Centre for Natural Sciences, Eötvös Loránd Research Network, Budapest, 1117, Hungary Department of Physiology, Faculty of Medicine, Semmelweis University, Budapest, 1094, Hungary Export Date: 29 December 2021 Correspondence Address: Simon, I.; Institute of Enzymology, Hungary; email: simon....</pre> </div></div>