دورية أكاديمية
Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins
| العنوان: | Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins |
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| المؤلفون: | Greta Bianchi, Marco Mangiagalli, Alberto Barbiroli, Sonia Longhi, Rita Grandori, Carlo Santambrogio, Stefania Brocca |
| المساهمون: | G. Bianchi, M. Mangiagalli, A.G. Barbiroli, S. Longhi, R. Grandori, C. Santambrogio, S. Brocca |
| بيانات النشر: | MDPI |
| سنة النشر: | 2022 |
| المجموعة: | The University of Milan: Archivio Istituzionale della Ricerca (AIR) |
| مصطلحات موضوعية: | average shape of conformational ensemble, charge clustering, charged-residue patterning, conformational compactne, ellipsoid model, hydrodynamic radiu, polyelectrolyte, proline content, solvent-accessible surface area, Settore BIO/10 - Biochimica |
| الوصف: | Intrinsically disordered proteins (IDPs) are ensembles of interconverting conformers whose conformational properties are governed by several physico-chemical factors, including their amino acid composition and the arrangement of oppositely charged residues within the primary structure. In this work, we investigate the effects of charge patterning on the average compactness and shape of three model IDPs with different proline content. We model IDP ensemble conformations as ellipsoids, whose size and shape are calculated by combining data from size-exclusion chromatography and native mass spectrometry. For each model IDP, we analyzed the wild-type protein and two synthetic variants with permuted positions of charged residues, where positive and negative amino acids are either evenly distributed or segregated. We found that charge clustering induces remodeling of the conformational ensemble, promoting compaction and/or increasing spherical shape. Our data illustrate that the average shape and volume of the ensembles depend on the charge distribution. The potential effect of other factors, such as chain length, number of proline residues, and secondary structure content, is also discussed. This methodological approach is a straightforward way to model IDP average conformation and decipher the salient sequence attributes influencing IDP structural properties. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/35454150; info:eu-repo/semantics/altIdentifier/wos/WOS:000786122400001; volume:12; issue:4; firstpage:1; lastpage:15; numberofpages:15; journal:BIOMOLECULES; https://hdl.handle.net/2434/981069Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85127859345 |
| DOI: | 10.3390/biom12040561 |
| الإتاحة: | https://doi.org/10.3390/biom12040561Test https://hdl.handle.net/2434/981069Test |
| حقوق: | info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.95F7C732 |
| قاعدة البيانات: | BASE |
| DOI: | 10.3390/biom12040561 |
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