Relative stabilities of conserved and non-conserved structures in the OB-fold superfamily.

Relative stabilities of conserved and non-conserved structures in the OB-fold superfamily.
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DOI:
10.3390/ijms10052412
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发表时间:
2009-05-22
影响因子:
5.6
通讯作者:
Alexandrescu AT
Alexandrescu AT
中科院分区:
生物学2区
文献类型:
--
作者:
Guardino KM;Sheftic SR;Slattery RE;Alexandrescu AT

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OB折叠是基于β-桶基序的潜水员结构,通常补充了其他非保存的二级结构。在这项工作中,保守的β桶大于非保存段中的位点。目前被归类为OB折叠,以建立此效果的基础。网络模型。最高的敏感性。我们的结果表明,蛋白质结构的模型在构成基序的周围发展,在进化过程中对结构变化更具抵抗力。说明在保守和未经保守的结构之间稳定性展开的差异。
The OB-fold is a diverse structure superfamily based on a β-barrel motif that is often supplemented with additional non-conserved secondary structures. Previous deletion mutagenesis and NMR hydrogen exchange studies of three OB-fold proteins showed that the structural stabilities of sites within the conserved β-barrels were larger than sites in non-conserved segments. In this work we examined a database of 80 representative domain structures currently classified as OB-folds, to establish the basis of this effect. Residue-specific values were obtained for the number of Cα-Cα distance contacts, sequence hydrophobicities, crystallographic B-factors, and theoretical B-factors calculated from a Gaussian Network Model. All four parameters point to a larger average flexibility for the non-conserved structures compared to the conserved β-barrels. The theoretical B-factors and contact densities show the highest sensitivity. Our results suggest a model of protein structure evolution in which novel structural features develop at the periphery of conserved motifs. Core residues are more resistant to structural changes during evolution since their substitution would disrupt a larger number of interactions. Similar factors are likely to account for the differences in stability to unfolding between conserved and non-conserved structures.
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发表时间: 1991-04-01
影响因子: 11.1
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