Dataset Information

Dataset for the thermodynamic description for the NaF-KF-RbF-ZnF2 system.

ABSTRACT: This data article includes the supplementary database material for the manuscript "Thermodynamic description for the NaF-KF-RbF-ZnF2 system", (Tang et al., 2018). We present all the thermodynamic parameters used and optimized model parameters of the thermodynamic database of the NaF-KF-RbF-ZnF2 quaternary system, by which researchers can obtain the calculated phase diagrams. What?s more, the comparison of calculations with experimental lattice constants of all compounds and relative deviations of unit cell parameters between before and after structure optimization for the NaF-KF-RbF-ZnF2 system are demonstrated in this work. Meanwhile, we provide the calculated mixing enthalpy in the binary AF-ZnF2 (A=Na, K and Rb) and AF-RbF (A=Na and K) system, which are helpful for researchers to better understand the system. These supplementary databases are most useful in understanding the manuscript (Tang et al., 2018).

SUBMITTER: Yin H

PROVIDER: S-EPMC6376127 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

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Dataset for the thermodynamic description for the NaF-KF-RbF-ZnF2 system.

Yin Huiqin H Wu Shuang S Wang Xueliang X Yan Long L Liu Wenguan W Tang Zhongfeng Z

Data in brief 20181105

This data article includes the supplementary database material for the manuscript "Thermodynamic description for the NaF-KF-RbF-ZnF2 system", (Tang et al., 2018). We present all the thermodynamic parameters used and optimized model parameters of the thermodynamic database of the NaF-KF-RbF-ZnF2 quaternary system, by which researchers can obtain the calculated phase diagrams. What׳s more, the comparison of calculations with experimental lattice constants of all compounds and ...[more]

PMID: 30809557

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Project description:Proteins from thermophiles are generally more thermostable than their mesophilic homologs, but little is known about the evolutionary process driving these differences. Here we attempt to understand how the diverse thermostabilities of bacterial ribonuclease H1 (RNH) proteins evolved. RNH proteins from Thermus thermophilus (ttRNH) and Escherichia coli (ecRNH) share similar structures but differ in melting temperature (T(m)) by 20 °C. ttRNH's greater stability is caused in part by the presence of residual structure in the unfolded state, which results in a low heat capacity of unfolding (ΔCp) relative to ecRNH. We first characterized RNH proteins from a variety of extant bacteria and found that Tm correlates with the species' growth temperatures, consistent with environmental selection for stability. We then used ancestral sequence reconstruction to statistically infer evolutionary intermediates along lineages leading to ecRNH and ttRNH from their common ancestor, which existed approximately 3 billion years ago. Finally, we synthesized and experimentally characterized these intermediates. The shared ancestor has a melting temperature between those of ttRNH and ecRNH; the T(m)s of intermediate ancestors along the ttRNH lineage increased gradually over time, while the ecRNH lineage exhibited an abrupt drop in Tm followed by relatively little change. To determine whether the underlying mechanisms for thermostability correlate with the changes in T(m), we measured the thermodynamic basis for stabilization--ΔCp and other thermodynamic parameters--for each of the ancestors. We observed that, while the T(m) changes smoothly, the mechanistic basis for stability fluctuates over evolutionary time. Thus, even while overall stability appears to be strongly driven by selection, the proteins explored a wide variety of mechanisms of stabilization, a phenomenon we call "thermodynamic system drift." This suggests that even on lineages with strong selection to increase stability, proteins have wide latitude to explore sequence space, generating biophysical diversity and potentially opening new evolutionary pathways.

Dataset Information

Dataset for the thermodynamic description for the NaF-KF-RbF-ZnF2 system.

Publications

Dataset for the thermodynamic description for the NaF-KF-RbF-ZnF<sub>2</sub> system.

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