The CBL1 protein is an important class of calcium signal proteins, which can response to drought, low temperature, high pH and other environmental stress. The differential scanning calorimetry was applied to study thermal properties of CBL1 protein from Populus during -30℃ to 0℃ and 20℃ to 95℃. It was found that although the CBL1 protein from Populus played a role in response to low temperature stress, but itself did not have frost resistance, meanwhile in the melting process, the ice content and temperature fitted exponential relationship. During the heating process, the irreversible denaturation temperature of CBL1 protein was about 81.6℃, meanwhile the performance of the entropy and enthalpy decreased in increments when it was below the denaturation temperature, and once climbed up to the denaturation temperature, the entropy and enthalpy increased rapidly, which showed a high thermal stability of CBL1 protein from Populus.
Key words
CBL1 protein of Populus; differential scanning calorimetry (DSC); entropy; enthalpy
{{custom_keyword}} /
{{custom_sec.title}}
{{custom_sec.title}}
{{custom_sec.content}}
References
[1] 杨昌友.新疆植物志[M].乌鲁木齐:新疆科技卫生出版社,1992:125- 127.
[2] Luan S. The CBL- CIPK network in plant calcium signaling[J]. Trends in plant science,2009,14(1):37-42.
[3] Luan S, Kudla J, Rodriguez-Concepcion M, et al. Calmodulins and calcineurin B- like proteins calcium sensors for specific signal response coupling in plants[J].The Plant Cell Online,2002,14(1):389- 400.
[4] Batistic O, Kudla J. Integration and channeling of calcium signaling through the CBL calcium sensor/CIPK protein kinase network[J].Planta,2004,219(6): 915-924.
[5] Kolukisaoglu ü, Weinl S, Blazevic D, et al. Calcium sensors and their interacting protein kinases: genomics of the Arabidopsis and rice CBL-CIPK signaling networks[J].Plant Physiology,2004,134(1): 43-58.
[6] Shang G, Cang H, Liu Z, et al. Crystallization and preliminary crystallographic analysis of a calcineurin B- like protein 1 (CBL1) mutant from Ammopiptanthus mongolicus[J].Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2010,66(12):1602-1605.
[7] 卢雁,李向荣.蛋白质变性机理与变性时的热力学参数研究进展[J].化学进展,2005,17(5):905-910.
[8] Wen J, Arthur K, Chemmalil L, et al. Applications of differential scanning calorimetry for thermal stability analysis of proteins: qualification of DSC[J].Journal of pharmaceutical sciences,2012,101 (3):955-964.
[9] 周晓蕾,陈滔滔,王保怀,等.沙冬青抗冻蛋白热滞活性的 DSC研究[J].物理化学学报,2001,17(1):66-69.
[10] Calavia M C, Burgos J. Thermal denaturation of ovine β- lactoglobulin[J].Journal of dairy science,1998,81(10):2572-2579.
[11] 张超,赵晓燕,马越,等.使用差示扫描量热仪测定抗冻蛋白热滞活性方法的研究[J].生物物理学报,2008,24(6):465-473.
[12] Salvetti G, Tombari E, Mikheeva L, et al. The endothermic effects during denaturation of lysozyme by temperature modulated calorimetry and an intermediate reaction equilibrium[J].The Journal of Physical Chemistry B,2002,106(23):6081-6087.
[13] Raymond J A, DeVries A L. Adsorption inhibition as a mechanism of freezing resistance in polar fishes[J].Proceedings of the National Academy of Sciences,1977,74(6):2589-2593.
[14] Characterising protein stability by DSC, Life Sciences Application Note[Z].Document number 20211021306 February 2006, Calorimetry Sciences Corporation.
[15] Wolynes P G. Energy landscapes and solved protein- folding problems[J].Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences,2005,363(1827): 453-467.
{{custom_fnGroup.title_en}}
Footnotes
{{custom_fn.content}}
