Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides
Background: Intrinsically disordered proteins and protein regions (IDPs/IDRs) are important in diverse biological processes. Lacking a stable secondary structure, they display an ensemble of conformations. One factor contributing to this conformational heterogeneity is the proline cis/trans isomeriz...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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IMR Press
2023-06-01
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| Series: | Frontiers in Bioscience-Landmark |
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| Online Access: | https://www.imrpress.com/journal/FBL/28/6/10.31083/j.fbl2806127 |
| _version_ | 1827910054729220096 |
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| author | Fanni Sebák János Szolomájer Nándor Papp Gábor K. Tóth Andrea Bodor |
| author_facet | Fanni Sebák János Szolomájer Nándor Papp Gábor K. Tóth Andrea Bodor |
| author_sort | Fanni Sebák |
| collection | DOAJ |
| description | Background: Intrinsically disordered proteins and protein regions (IDPs/IDRs) are important in diverse biological processes. Lacking a stable secondary structure, they display an ensemble of conformations. One factor contributing to this conformational heterogeneity is the proline cis/trans isomerization. The knowledge and value of a given cis/trans proline ratio are paramount, as the different conformational states can be responsible for different biological functions. Nuclear Magnetic Resonance (NMR) spectroscopy is the only method to characterize the two co-existing isomers on an atomic level, and only a few works report on these data. Methods: After collecting the available experimental literature findings, we conducted a statistical analysis regarding the influence of the neighboring amino acid types (i ± 4 regions) on forming a cis-Pro isomer. Based on this, several regularities were formulated. NMR spectroscopy was then used to define the cis-Pro content on model peptides and desired point mutations. Results: Analysis of NMR spectra prove the dependence of the cis-Pro content on the type of the neighboring amino acid—with special attention on aromatic and positively charged sidechains. Conclusions: Our results may benefit the design of protein regions with a given cis-Pro content, and contribute to a better understanding of the roles and functions of IDPs. |
| first_indexed | 2024-03-13T01:46:44Z |
| format | Article |
| id | doaj.art-9297d52267314cd884801632739d0af5 |
| institution | Directory Open Access Journal |
| issn | 2768-6701 |
| language | English |
| last_indexed | 2024-03-13T01:46:44Z |
| publishDate | 2023-06-01 |
| publisher | IMR Press |
| record_format | Article |
| series | Frontiers in Bioscience-Landmark |
| spelling | doaj.art-9297d52267314cd884801632739d0af52023-07-03T07:33:50ZengIMR PressFrontiers in Bioscience-Landmark2768-67012023-06-0128612710.31083/j.fbl2806127S2768-6701(23)00908-5Proline cis/trans Isomerization in Intrinsically Disordered Proteins and PeptidesFanni Sebák0János Szolomájer1Nándor Papp2Gábor K. Tóth3Andrea Bodor4Analytical and BioNMR Laboratory, Institute of Chemistry, Eötvös Loránd University, 1117 Budapest, HungaryDepartment of Medical Chemistry, University of Szeged, 6720 Szeged, HungaryAnalytical and BioNMR Laboratory, Institute of Chemistry, Eötvös Loránd University, 1117 Budapest, HungaryDepartment of Medical Chemistry, University of Szeged, 6720 Szeged, HungaryAnalytical and BioNMR Laboratory, Institute of Chemistry, Eötvös Loránd University, 1117 Budapest, HungaryBackground: Intrinsically disordered proteins and protein regions (IDPs/IDRs) are important in diverse biological processes. Lacking a stable secondary structure, they display an ensemble of conformations. One factor contributing to this conformational heterogeneity is the proline cis/trans isomerization. The knowledge and value of a given cis/trans proline ratio are paramount, as the different conformational states can be responsible for different biological functions. Nuclear Magnetic Resonance (NMR) spectroscopy is the only method to characterize the two co-existing isomers on an atomic level, and only a few works report on these data. Methods: After collecting the available experimental literature findings, we conducted a statistical analysis regarding the influence of the neighboring amino acid types (i ± 4 regions) on forming a cis-Pro isomer. Based on this, several regularities were formulated. NMR spectroscopy was then used to define the cis-Pro content on model peptides and desired point mutations. Results: Analysis of NMR spectra prove the dependence of the cis-Pro content on the type of the neighboring amino acid—with special attention on aromatic and positively charged sidechains. Conclusions: Our results may benefit the design of protein regions with a given cis-Pro content, and contribute to a better understanding of the roles and functions of IDPs.https://www.imrpress.com/journal/FBL/28/6/10.31083/j.fbl2806127intrinsically disordered proteinsnmr spectroscopyprolinecis/trans isomerizationstatistical analysis |
| spellingShingle | Fanni Sebák János Szolomájer Nándor Papp Gábor K. Tóth Andrea Bodor Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides Frontiers in Bioscience-Landmark intrinsically disordered proteins nmr spectroscopy proline cis/trans isomerization statistical analysis |
| title | Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides |
| title_full | Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides |
| title_fullStr | Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides |
| title_full_unstemmed | Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides |
| title_short | Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides |
| title_sort | proline cis trans isomerization in intrinsically disordered proteins and peptides |
| topic | intrinsically disordered proteins nmr spectroscopy proline cis/trans isomerization statistical analysis |
| url | https://www.imrpress.com/journal/FBL/28/6/10.31083/j.fbl2806127 |
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