دورية أكاديمية
Stabilizing salt-bridge enhances protein thermostability by reducing the heat capacity change of unfolding.
العنوان: | Stabilizing salt-bridge enhances protein thermostability by reducing the heat capacity change of unfolding. |
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المؤلفون: | Chi-Ho Chan, Tsz-Ha Yu, Kam-Bo Wong |
المصدر: | PLoS ONE, Vol 6, Iss 6, p e21624 (2011) |
بيانات النشر: | Public Library of Science (PLoS), 2011. |
سنة النشر: | 2011 |
المجموعة: | LCC:Medicine LCC:Science |
مصطلحات موضوعية: | Medicine, Science |
الوصف: | Most thermophilic proteins tend to have more salt bridges, and achieve higher thermostability by up-shifting and broadening their protein stability curves. While the stabilizing effect of salt-bridge has been extensively studied, experimental data on how salt-bridge influences protein stability curves are scarce. Here, we used double mutant cycles to determine the temperature-dependency of the pair-wise interaction energy and the contribution of salt-bridges to ΔC(p) in a thermophilic ribosomal protein L30e. Our results showed that the pair-wise interaction energies for the salt-bridges E6/R92 and E62/K46 were stabilizing and insensitive to temperature changes from 298 to 348 K. On the other hand, the pair-wise interaction energies between the control long-range ion-pair of E90/R92 were negligible. The ΔC(p) of all single and double mutants were determined by Gibbs-Helmholtz and Kirchhoff analyses. We showed that the two stabilizing salt-bridges contributed to a reduction of ΔC(p) by 0.8-1.0 kJ mol⁻¹ K⁻¹. Taken together, our results suggest that the extra salt-bridges found in thermophilic proteins enhance the thermostability of proteins by reducing ΔC(p), leading to the up-shifting and broadening of the protein stability curves. |
نوع الوثيقة: | article |
وصف الملف: | electronic resource |
اللغة: | English |
تدمد: | 1932-6203 |
العلاقة: | http://europepmc.org/articles/PMC3123365?pdf=renderTest; https://doaj.org/toc/1932-6203Test |
DOI: | 10.1371/journal.pone.0021624 |
الوصول الحر: | https://doaj.org/article/63b32f18ab29467488423aaa2dbb527bTest |
رقم الانضمام: | edsdoj.63b32f18ab29467488423aaa2dbb527b |
قاعدة البيانات: | Directory of Open Access Journals |
تدمد: | 19326203 |
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DOI: | 10.1371/journal.pone.0021624 |