Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins
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...
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| Format: | Article |
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MDPI AG
2021-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/24/13404 |
| _version_ | 1797503808445612032 |
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| author | Csaba Magyar Anikó Mentes Miklós Cserző István Simon |
| author_facet | Csaba Magyar Anikó Mentes Miklós Cserző István Simon |
| author_sort | Csaba Magyar |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T03:55:38Z |
| format | Article |
| id | doaj.art-6fce9e8d532c4a4ea05c7936cc57f143 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T03:55:38Z |
| publishDate | 2021-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-6fce9e8d532c4a4ea05c7936cc57f1432023-11-23T08:45:52ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-12-0122241340410.3390/ijms222413404Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding ProteinsCsaba Magyar0Anikó Mentes1Miklós Cserző2István Simon3Institute of Enzymology, Research Centre for Natural Sciences, Eötvös Loránd Research Network, 1117 Budapest, HungaryInstitute of Enzymology, Research Centre for Natural Sciences, Eötvös Loránd Research Network, 1117 Budapest, HungaryInstitute of Enzymology, Research Centre for Natural Sciences, Eötvös Loránd Research Network, 1117 Budapest, HungaryInstitute of Enzymology, Research Centre for Natural Sciences, Eötvös Loránd Research Network, 1117 Budapest, HungaryMutual 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.https://www.mdpi.com/1422-0067/22/24/13404intrinsically disordered proteinsmutual synergetic foldingsolvent accessibility of peptide bondsinter-subunit interactionsolvent-accessible surface areaShannon information entropy |
| spellingShingle | Csaba Magyar Anikó Mentes Miklós Cserző István Simon Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins International Journal of Molecular Sciences intrinsically disordered proteins mutual synergetic folding solvent accessibility of peptide bonds inter-subunit interaction solvent-accessible surface area Shannon information entropy |
| title | Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins |
| title_full | Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins |
| title_fullStr | Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins |
| title_full_unstemmed | Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins |
| title_short | Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins |
| title_sort | origin of increased solvent accessibility of peptide bonds in mutual synergetic folding proteins |
| topic | intrinsically disordered proteins mutual synergetic folding solvent accessibility of peptide bonds inter-subunit interaction solvent-accessible surface area Shannon information entropy |
| url | https://www.mdpi.com/1422-0067/22/24/13404 |
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