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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Autor*in:	Csaba Magyar [verfasserIn] Anikó Mentes [verfasserIn] Miklós Cserző [verfasserIn] István Simon [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	intrinsically disordered proteins mutual synergetic folding solvent accessibility of peptide bonds inter-subunit interaction solvent-accessible surface area Shannon information entropy

Übergeordnetes Werk:	In: International Journal of Molecular Sciences - MDPI AG, 2003, 22(2021), 24, p 13404
Übergeordnetes Werk:	volume:22 ; year:2021 ; number:24, p 13404

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc Journal toc

DOI / URN:	10.3390/ijms222413404

Katalog-ID:	DOAJ014180499

Internformat


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spelling	10.3390/ijms222413404 doi (DE-627)DOAJ014180499 (DE-599)DOAJ6fce9e8d532c4a4ea05c7936cc57f143 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Csaba Magyar verfasserin aut Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. intrinsically disordered proteins mutual synergetic folding solvent accessibility of peptide bonds inter-subunit interaction solvent-accessible surface area Shannon information entropy Biology (General) Chemistry Anikó Mentes verfasserin aut Miklós Cserző verfasserin aut István Simon verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 22(2021), 24, p 13404 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:22 year:2021 number:24, p 13404 https://doi.org/10.3390/ijms222413404 kostenfrei https://doaj.org/article/6fce9e8d532c4a4ea05c7936cc57f143 kostenfrei https://www.mdpi.com/1422-0067/22/24/13404 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 22 2021 24, p 13404
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allfieldsSound	10.3390/ijms222413404 doi (DE-627)DOAJ014180499 (DE-599)DOAJ6fce9e8d532c4a4ea05c7936cc57f143 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Csaba Magyar verfasserin aut Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. intrinsically disordered proteins mutual synergetic folding solvent accessibility of peptide bonds inter-subunit interaction solvent-accessible surface area Shannon information entropy Biology (General) Chemistry Anikó Mentes verfasserin aut Miklós Cserző verfasserin aut István Simon verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 22(2021), 24, p 13404 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:22 year:2021 number:24, p 13404 https://doi.org/10.3390/ijms222413404 kostenfrei https://doaj.org/article/6fce9e8d532c4a4ea05c7936cc57f143 kostenfrei https://www.mdpi.com/1422-0067/22/24/13404 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 22 2021 24, p 13404
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callnumber-first	Q - Science
author	Csaba Magyar
spellingShingle	Csaba Magyar misc QH301-705.5 misc QD1-999 misc intrinsically disordered proteins misc mutual synergetic folding misc solvent accessibility of peptide bonds misc inter-subunit interaction misc solvent-accessible surface area misc Shannon information entropy misc Biology (General) misc Chemistry Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins
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topic_title	QH301-705.5 QD1-999 Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins intrinsically disordered proteins mutual synergetic folding solvent accessibility of peptide bonds inter-subunit interaction solvent-accessible surface area Shannon information entropy
topic	misc QH301-705.5 misc QD1-999 misc intrinsically disordered proteins misc mutual synergetic folding misc solvent accessibility of peptide bonds misc inter-subunit interaction misc solvent-accessible surface area misc Shannon information entropy misc Biology (General) misc Chemistry
topic_unstemmed	misc QH301-705.5 misc QD1-999 misc intrinsically disordered proteins misc mutual synergetic folding misc solvent accessibility of peptide bonds misc inter-subunit interaction misc solvent-accessible surface area misc Shannon information entropy misc Biology (General) misc Chemistry
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title	Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins
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title_full	Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins
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title_sort	origin of increased solvent accessibility of peptide bonds in mutual synergetic folding proteins
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title_auth	Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins
abstract	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.
abstractGer	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.
abstract_unstemmed	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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container_issue	24, p 13404
title_short	Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins
url	https://doi.org/10.3390/ijms222413404 https://doaj.org/article/6fce9e8d532c4a4ea05c7936cc57f143 https://www.mdpi.com/1422-0067/22/24/13404 https://doaj.org/toc/1661-6596 https://doaj.org/toc/1422-0067
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up_date	2024-07-03T21:41:44.197Z
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Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins

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