Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR
| Autor: | Yinshan Yang, Vincent Van Deuren, Christian Roumestand, Catherine Anne Royer, Philippe Barthe, Cécile Dubois, Karine de Guillen |
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| Přispěvatelé: | Centre de Biochimie Structurale [Montpellier] (CBS), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Rensselaer Polytechnic Institute (RPI), ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), BARTHE, Philippe, Infrastructure Française pour la Biologie Structurale Intégrée - - FRISBI2010 - ANR-10-INBS-0005 - INBS - VALID |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Life Sciences & Biomedicine - Other Topics
DYNAMICS 0301 basic medicine [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] STAPHYLOCOCCAL NUCLEASE Stereochemistry QH301-705.5 [SDV]Life Sciences [q-bio] Hydrostatic pressure Sequence (biology) Biology 010402 general chemistry SEQUENCE 01 natural sciences General Biochemistry Genetics and Molecular Biology Article 03 medical and health sciences chemistry.chemical_compound Amide protein folding Molecule Biology (General) ENERGY LANDSCAPE Science & Technology SPECTROSCOPY [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] STABILITY General Immunology and Microbiology high hydrostatic pressure NMR 0104 chemical sciences Folding (chemistry) 030104 developmental biology STATES chemistry Yield (chemistry) thermodynamic stability Chemical stability Protein folding General Agricultural and Biological Sciences Life Sciences & Biomedicine |
| Zdroj: | Biology Biology, MDPI 2021, 10 (7), pp.656. ⟨10.3390/biology10070656⟩ Biology, Vol 10, Iss 656, p 656 (2021) Volume 10 Issue 7 Biology, 2021, 10 (7), pp.656. ⟨10.3390/biology10070656⟩ |
| ISSN: | 2079-7737 |
| DOI: | 10.3390/biology10070656⟩ |
| Popis: | Simple Summary During the last decade, high-pressure multidimensional NMR has emerged as a very powerful tool to describe the folding landscapes of proteins. This is (i) because pressure is a gentle perturbation, the effects of which originate from local properties of the folded state, contrary to chemical or thermal denaturation, and (ii) because multidimensional NMR intrinsically provides multiple probes strategically scattered on the three-dimensional structure of the protein, allowing a quasi-atomic resolution to describe the folding pathway. Residue-specific information obtained from these probes can be used to describe protein folding pathways through the calculation of NMR-derived fractional probabilities of contact at increasing pressure. Here, we used this strategy to evaluate and compare the results obtained from NH amide, CαHα, and CH3 groups when used as NMR probes to explore the folding pathway of the model protein ∆+PHS Staphylococcal Nuclease. Abstract Multidimensional NMR intrinsically provides multiple probes that can be used for deciphering the folding pathways of proteins: NH amide and CαHα groups are strategically located on the backbone of the protein, while CH3 groups, on the side-chain of methylated residues, are involved in important stabilizing interactions in the hydrophobic core. Combined with high hydrostatic pressure, these observables provide a powerful tool to explore the conformational landscapes of proteins. In the present study, we made a comparative assessment of the NH, CαHα, and CH3 groups for analyzing the unfolding pathway of ∆+PHS Staphylococcal Nuclease. These probes yield a similar description of the folding pathway, with virtually identical thermodynamic parameters for the unfolding reaction, despite some notable differences. Thus, if partial unfolding begins at identical pressure for these observables (especially in the case of backbone probes) and concerns similar regions of the molecule, the residues involved in contact losses are not necessarily the same. In addition, an unexpected slight shift toward higher pressure was observed in the sequence of the scenario of unfolding with CαHα when compared to amide groups. |
| Databáze: | OpenAIRE |
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