دورية أكاديمية
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Structural and thermodynamic analysis of factors governing the stability and thermal folding/unfolding of SazCA.

التفاصيل البيبلوغرافية
العنوان: Structural and thermodynamic analysis of factors governing the stability and thermal folding/unfolding of SazCA.
المؤلفون: Kumar S; Quantum and Molecular Engineering Laboratory, Department of Chemical Engineering, Indian Institute of Technology Kharagpur, Kharagpur, India., Deshpande PA; Quantum and Molecular Engineering Laboratory, Department of Chemical Engineering, Indian Institute of Technology Kharagpur, Kharagpur, India.
المصدر: PloS one [PLoS One] 2021 Apr 15; Vol. 16 (4), pp. e0249866. Date of Electronic Publication: 2021 Apr 15 (Print Publication: 2021).
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science
مواضيع طبية MeSH: Protein Unfolding*, Bacteria/*enzymology , Bacterial Proteins/*chemistry , Carbonic Anhydrases/*chemistry, Enzyme Stability ; Molecular Dynamics Simulation
مستخلص: Molecular basis of protein stability at different temperatures is a fundamental problem in protein science that is substantially far from being accurately and quantitatively solved as it requires an explicit knowledge of the temperature dependence of folding free energy of amino acid residues. In the present study, we attempted to gain insights into the thermodynamic stability of SazCA and its implications on protein folding/unfolding. We report molecular dynamics simulations of water solvated SazCA in a temperature range of 293-393 K to study the relationship between the thermostability and flexibility. Our structural analysis shows that the protein maintains the highest structural stability at 353 K and the protein conformations are highly flexible at temperatures above 353 K. Larger exposure of hydrophobic surface residues to the solvent medium for conformations beyond 353 K were identified from H-bond analysis. Higher number of secondary structure contents exhibited by SazCA at 353 K corroborated the conformations at 353 K to exhibit the highest thermal stability. The analysis of thermodynamics of protein stability revealed that the conformations that denature at higher melting temperatures tend to have greater maximum thermal stability. Our analysis shows that 353 K conformations have the highest melting temperature, which was found to be close to the experimental optimum temperature. The enhanced protein stability at 353 K due the least value of heat capacity at unfolding suggested an increase in folding. Comparative Gibbs free energy analysis and funnel shaped energy landscape confirmed a transition in folding/unfolding pathway of SazCA at 353 K.
Competing Interests: The authors have declared that no competing interests exist.
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المشرفين على المادة: 0 (Bacterial Proteins)
EC 4.2.1.1 (Carbonic Anhydrases)
SCR Organism: Sulfurihydrogenibium azorense
تواريخ الأحداث: Date Created: 20210415 Date Completed: 20210922 Latest Revision: 20240331
رمز التحديث: 20240331
مُعرف محوري في PubMed: PMC8049272
DOI: 10.1371/journal.pone.0249866
PMID: 33857217
قاعدة البيانات: MEDLINE
الوصف
تدمد:1932-6203
DOI:10.1371/journal.pone.0249866