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在生物膜中测量的跨膜螺旋相互作用的稳定性。

The stability of transmembrane helix interactions measured in a biological membrane.

作者信息

Finger Carmen, Volkmer Thomas, Prodöhl Alexander, Otzen Daniel E, Engelman Donald M, Schneider Dirk

机构信息

Institut für Biochemie und Molekularbiologie, Albert-Ludwigs-Universität Freiburg, Stefan-Meier-Strasse 19, 79104 Freiburg, Germany.

出版信息

J Mol Biol. 2006 May 19;358(5):1221-8. doi: 10.1016/j.jmb.2006.02.065. Epub 2006 Mar 13.

Abstract

Despite some promising progress in the understanding of membrane protein folding and assembly, there is little experimental information regarding the thermodynamic stability of transmembrane helix interactions and even less on the stability of transmembrane helix-helix interactions in a biological membrane. Here we describe an approach that allows quantitative measurement of transmembrane helix interactions in a biological membrane, and calculation of changes in the interaction free energy resulting from substitution of single amino acids. Dimerization of several variants of the glycophorin A transmembrane domain are characterized and compared to the wild-type (wt) glycophorin A transmembrane helix dimerization. The calculated DeltaDeltaG(app) values are further compared with values found in the literature. In addition, we compare interactions between the wt glycophorin A transmembrane domain and helices in which critical glycine residues are replaced by alanine or serine, respectively. The data demonstrate that replacement of the glycine residues by serine is less destabilizing than replacement by alanine with a DeltaDeltaG(app) value of about 0.4 kcal/mol. Our study comprises the first measurement of a transmembrane helix interaction in a biological membrane, and we are optimistic that it can be further developed and applied.

摘要

尽管在膜蛋白折叠和组装的理解方面取得了一些有前景的进展,但关于跨膜螺旋相互作用的热力学稳定性的实验信息很少,而关于生物膜中跨膜螺旋 - 螺旋相互作用稳定性的信息更少。在这里,我们描述了一种方法,该方法允许定量测量生物膜中的跨膜螺旋相互作用,并计算单个氨基酸取代导致的相互作用自由能的变化。对血型糖蛋白A跨膜结构域的几种变体的二聚化进行了表征,并与野生型(wt)血型糖蛋白A跨膜螺旋二聚化进行了比较。计算得到的ΔΔG(app)值进一步与文献中的值进行了比较。此外,我们比较了wt血型糖蛋白A跨膜结构域与其中关键甘氨酸残基分别被丙氨酸或丝氨酸取代的螺旋之间的相互作用。数据表明,用丝氨酸取代甘氨酸残基比用丙氨酸取代的去稳定作用更小,ΔΔG(app)值约为0.4千卡/摩尔。我们的研究包括对生物膜中跨膜螺旋相互作用的首次测量,我们乐观地认为它可以进一步发展和应用。

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