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Biological Roles of Protein Kinetic Stability
Biochemistry ( IF 2.9 ) Pub Date : 2017-11-13 00:00:00 , DOI: 10.1021/acs.biochem.7b00942 Wilfredo Colón 1 , Jennifer Church 1 , Jayeeta Sen 1 , Jane Thibeault 1 , Hannah Trasatti 1 , Ke Xia 1
Biochemistry ( IF 2.9 ) Pub Date : 2017-11-13 00:00:00 , DOI: 10.1021/acs.biochem.7b00942 Wilfredo Colón 1 , Jennifer Church 1 , Jayeeta Sen 1 , Jane Thibeault 1 , Hannah Trasatti 1 , Ke Xia 1
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A protein’s stability may range from nonexistent, as in the case of intrinsically disordered proteins, to very high, as indicated by a protein’s resistance to degradation, even under relatively harsh conditions. The stability of this latter group is usually under kinetic control because of a high activation energy for unfolding that virtually traps the protein in a specific conformation, thereby conferring resistance to proteolytic degradation and misfolding aggregation. The usual outcome of kinetic stability is a longer protein half-life. Thus, the protective role of protein kinetic stability is often appreciated, but relatively little is known about the extent of biological roles related to this property. In this Perspective, we will discuss several known or putative biological roles of protein kinetic stability, including protection from stressors to avoid aggregation or premature degradation, achieving long-term phenotypic change, and regulating cellular processes by controlling the trigger and timing of molecular motion. The picture that emerges from this analysis is that protein kinetic stability is involved in a myriad of known and yet to be discovered biological functions via its ability to confer degradation resistance and control the timing, extent, and permanency of molecular motion.
中文翻译：
蛋白质动力学稳定性的生物学作用
蛋白质的稳定性可能从不存在（如在本质上无序的蛋白质的情况下）到很高的（如在相对苛刻的条件下，由蛋白质对降解的抵抗力所表明）。后一组的稳定性通常在动力学控制下，因为用于展开的高活化能实际上将蛋白质捕获为特定构象，从而赋予了对蛋白水解降解和错误折叠聚集的抵抗力。动力学稳定性的通常结果是更长的蛋白质半衰期。因此，人们常常认识到蛋白质动力学稳定性的保护作用，但是关于与该性质有关的生物学作用的程度知之甚少。在这一观点中，我们将讨论蛋白质动力学稳定性的几种已知或推定的生物学作用，包括防止应激源以避免聚集或过早降解，实现长期表型变化，以及通过控制分子运动的触发和时机来调节细胞过程。通过这种分析得出的结论是，蛋白质动力学稳定性通过其赋予降解抗性和控制分子运动的时间，程度和永久性的能力而参与了众多已知的和尚未发现的生物学功能。
更新日期：2017-11-13
中文翻译：
蛋白质动力学稳定性的生物学作用
蛋白质的稳定性可能从不存在（如在本质上无序的蛋白质的情况下）到很高的（如在相对苛刻的条件下，由蛋白质对降解的抵抗力所表明）。后一组的稳定性通常在动力学控制下，因为用于展开的高活化能实际上将蛋白质捕获为特定构象，从而赋予了对蛋白水解降解和错误折叠聚集的抵抗力。动力学稳定性的通常结果是更长的蛋白质半衰期。因此，人们常常认识到蛋白质动力学稳定性的保护作用，但是关于与该性质有关的生物学作用的程度知之甚少。在这一观点中，我们将讨论蛋白质动力学稳定性的几种已知或推定的生物学作用，包括防止应激源以避免聚集或过早降解，实现长期表型变化，以及通过控制分子运动的触发和时机来调节细胞过程。通过这种分析得出的结论是，蛋白质动力学稳定性通过其赋予降解抗性和控制分子运动的时间，程度和永久性的能力而参与了众多已知的和尚未发现的生物学功能。
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