Shan-shan Li, Ying-ying Yu, De-yong Li, Xiao-chuan He, Yong-zhen Bao, Yu-xiang Weng. Thermal-induced Unfolding of β-Crystallin and Disassembly of its Oligomers Revealed by Temperature-Jump Time-Resolved Infrared Spectroscopy[J]. Chinese Journal of Chemical Physics , 2013, 26(6): 739-746. doi: 10.1063/1674-0068/26/06/739-746
Citation: Shan-shan Li, Ying-ying Yu, De-yong Li, Xiao-chuan He, Yong-zhen Bao, Yu-xiang Weng. Thermal-induced Unfolding of β-Crystallin and Disassembly of its Oligomers Revealed by Temperature-Jump Time-Resolved Infrared Spectroscopy[J]. Chinese Journal of Chemical Physics , 2013, 26(6): 739-746. doi: 10.1063/1674-0068/26/06/739-746

Thermal-induced Unfolding of β-Crystallin and Disassembly of its Oligomers Revealed by Temperature-Jump Time-Resolved Infrared Spectroscopy

doi: 10.1063/1674-0068/26/06/739-746
Funds:  This work was supported by the National Natural Science Foundation of China (No.20925313, No.21090342, and No.21173012) and the National Basic Research Program of China (No.2006CB910302)
  • β-Crystallins are the major structural proteins existing in the vertebrate lens, and their conformational stability is critical in maintaining the life-long transparency and refraction index of the lens. Seven subunits of β-crystallins naturally assemble into various heteroge-neous oligomers with different sizes. Here, we systematically investigated the thermal sta-bility of the different secondary structures present in β-crystallins and then the dynamic process for the thermal-induced unfolding of β-crystallins by Fourier transform infrared spectroscopy-monitored thermal titration and temperature-jump nanosecond time-resolved IR difference absorbance spectra. Our results show that the N-terminal anti-parallel β-sheets in β-crystallin are the most unstable with a transition midpoint temperature at 36.0±2.1 oC, leading to the formation of an intermediate consisting vastly of random coil structures. This intermediate structure is temporally assigned to that of the monomer generated by the thermal-induced disassembly of β-crystallin oligomers with a transition midpoint tempera-ture of 40.4±0.7 oC. The global unfolding of β-crystallins that leads to denaturation and aggregation indicated by the formation of intermolecular anti-parallel β-sheets has a transi-tion midpoint temperature determined as 72.4±0.2 oC. Temperature-jump time-resolved IR absorbance difference spectroscopy analysis further reveals that thermal-induced unfolding of β-crystallins occurs firstly in the anti-parallel β-sheets in the N-terminal domains with a time constant of 50 ns
  • 加载中
  • 加载中
通讯作者: 陈斌, bchen63@163.com
  • 1. 

    沈阳化工大学材料科学与工程学院 沈阳 110142

  1. 本站搜索
  2. 百度学术搜索
  3. 万方数据库搜索
  4. CNKI搜索

Article Metrics

Article views(1479) PDF downloads(1193) Cited by()

Proportional views
Related

Thermal-induced Unfolding of β-Crystallin and Disassembly of its Oligomers Revealed by Temperature-Jump Time-Resolved Infrared Spectroscopy

doi: 10.1063/1674-0068/26/06/739-746
Funds:  This work was supported by the National Natural Science Foundation of China (No.20925313, No.21090342, and No.21173012) and the National Basic Research Program of China (No.2006CB910302)

Abstract: β-Crystallins are the major structural proteins existing in the vertebrate lens, and their conformational stability is critical in maintaining the life-long transparency and refraction index of the lens. Seven subunits of β-crystallins naturally assemble into various heteroge-neous oligomers with different sizes. Here, we systematically investigated the thermal sta-bility of the different secondary structures present in β-crystallins and then the dynamic process for the thermal-induced unfolding of β-crystallins by Fourier transform infrared spectroscopy-monitored thermal titration and temperature-jump nanosecond time-resolved IR difference absorbance spectra. Our results show that the N-terminal anti-parallel β-sheets in β-crystallin are the most unstable with a transition midpoint temperature at 36.0±2.1 oC, leading to the formation of an intermediate consisting vastly of random coil structures. This intermediate structure is temporally assigned to that of the monomer generated by the thermal-induced disassembly of β-crystallin oligomers with a transition midpoint tempera-ture of 40.4±0.7 oC. The global unfolding of β-crystallins that leads to denaturation and aggregation indicated by the formation of intermolecular anti-parallel β-sheets has a transi-tion midpoint temperature determined as 72.4±0.2 oC. Temperature-jump time-resolved IR absorbance difference spectroscopy analysis further reveals that thermal-induced unfolding of β-crystallins occurs firstly in the anti-parallel β-sheets in the N-terminal domains with a time constant of 50 ns

Shan-shan Li, Ying-ying Yu, De-yong Li, Xiao-chuan He, Yong-zhen Bao, Yu-xiang Weng. Thermal-induced Unfolding of β-Crystallin and Disassembly of its Oligomers Revealed by Temperature-Jump Time-Resolved Infrared Spectroscopy[J]. Chinese Journal of Chemical Physics , 2013, 26(6): 739-746. doi: 10.1063/1674-0068/26/06/739-746
Citation: Shan-shan Li, Ying-ying Yu, De-yong Li, Xiao-chuan He, Yong-zhen Bao, Yu-xiang Weng. Thermal-induced Unfolding of β-Crystallin and Disassembly of its Oligomers Revealed by Temperature-Jump Time-Resolved Infrared Spectroscopy[J]. Chinese Journal of Chemical Physics , 2013, 26(6): 739-746. doi: 10.1063/1674-0068/26/06/739-746

Catalog

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return