Hot and crowded: new insights into the dynamics of thermophilic enzymes from multiscale modeling.
Hot and crowded: new insights into the dynamics of thermophilic enzymes from multiscale modeling.
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炎热和拥挤：从多尺度建模对嗜热酶动力学的新见解。
DOI：
10.1016/j.bpj.2011.10.033
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发表时间：
2011
影响因子：
3.4
通讯作者：
Tobias,DouglasJ
中科院分区：
文献类型：
--
作者：
Heyden,Matthias;Tobias,DouglasJ
了解蛋白质的氨基酸序列如何决定其三维结构、动力学，并最终决定其生物功能仍然是最基本的生物物理学问题之一。虽然这个问题不太可能一蹴而就，但自然界的多样性本身为我们提供了一个解决这个问题的方法。对极端环境条件（如高温）的适应导致了嗜热酶的进化，这些酶不仅在60℃以上的温度下保持稳定，而且在高温下表现出最大的活性。值得注意的是，这些嗜热酶与中温酶仍然保持着相当程度的同源性，中温酶在中等温度下茁壮成长的物种中催化相同的反应。研究来自不同物种的中温/嗜热酶同源物，可以评估序列和结构的适度变化如何改变酶的性质，使其在高温下具有更高的热稳定性和高活性。这种比较还提供了对结构-功能关系的额外见解。
Understanding how the amino acid sequence of a protein determines its three-dimensional structure, dynamics, and, ultimately, its biological function remains one of the most fundamental biophysical problems. Although this problem is unlikely to be solved in a single step, one way of breaking it down is offered to us by nature’s diversity itself. Adaptation to extreme environmental conditions, eg, high temperatures, led to the evolution of thermophilic enzymes that are not only stable at temperatures beyond 60 C, but also exhibit their maximum activity at elevated temperatures. Remarkably, these thermophilic enzymes still maintain a significant degree of homology to their mesophilic counterparts, enzymes that catalyze the same reactions in species that thrive at moderate temperatures. Studying mesophilic/thermophilic enzyme homologs from different species side-by-side enables an assessment of how moderate changes in sequence and structure alter the enzyme’s properties toward higher thermostability and high activity at elevated temperatures. Such a comparison also provides additional insights into structure-function relationships in general.
溶液中蛋白质的亚纳秒动力学：分子动力学模拟和非弹性中子散射
DOI：
--
发表时间：
2006
期刊：
影响因子：
--
作者：
M. Tarek;D. Tobias
通讯作者：
D. Tobias
拥挤导致嗜热和嗜温蛋白质扩散的差异：中子散射结果的新视角。
影响因子：
3.4
作者：
E. Marcos;P. Mestres;R. Crehuet
通讯作者：
R. Crehuet