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链霉亲和素四聚化与二维结晶:一种平均场方法。

Streptavidin tetramerization and 2D crystallization: a mean-field approach.

作者信息

Coussaert T, Völkel A R, Noolandi J, Gast A P

机构信息

Department of Chemical Engineering, Stanford University, Stanford, California 94305-5025, USA.

出版信息

Biophys J. 2001 Apr;80(4):2004-10. doi: 10.1016/S0006-3495(01)76170-X.

Abstract

A mean-field theoretical approach is applied to streptavidin tetramerization and two-dimensional (2D) crystallization. This theory includes, in particular, solvent-residue interactions following the inhomogeneous Flory-Huggins model for polymers. It also takes into account residue-residue interactions by using tabulated pair interaction parameters. This theory allows one to explicitly calculate the entropy of the inhomogeneous system. We show that hydrophobic interactions are responsible for the stability of tetramerization. Within the present theory, the equilibrium distance between the two dimers is the same as that determined experimentally. The free energy of tetramerization (i.e., dissociation of the two dimers) is 50 k(B)T. Unlike tetramerization, hydrophobic interactions alone are not sufficient to stabilize the 2D crystal C(222), but solvent-mediated residue-residue interactions give the most important contribution.

摘要

一种平均场理论方法被应用于链霉亲和素的四聚化和二维(2D)结晶。该理论特别包括遵循聚合物非均匀弗洛里-哈金斯模型的溶剂-残基相互作用。它还通过使用列表化的对相互作用参数来考虑残基-残基相互作用。该理论允许明确计算非均匀系统的熵。我们表明疏水相互作用是四聚化稳定性的原因。在当前理论中,两个二聚体之间的平衡距离与实验确定的距离相同。四聚化的自由能(即两个二聚体的解离)为50k(B)T。与四聚化不同,仅疏水相互作用不足以稳定二维晶体C(222),但溶剂介导的残基-残基相互作用贡献最为重要。

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本文引用的文献

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Mean-field analysis of protein-protein interactions.
Biophys Chem. 1998 Nov 16;75(2):115-28. doi: 10.1016/s0301-4622(98)00201-4.
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Protein crystallization.蛋白质结晶
Annu Rev Phys Chem. 1996;47:171-204. doi: 10.1146/annurev.physchem.47.1.171.
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Principles of protein-protein recognition.蛋白质-蛋白质识别原理
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