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首页> 外文期刊>Biochemistry >Residue-Specific Description of Non-Native Transient Structures in the Ensemble of Acid-Denatured Structures of the All-β Protein c-src SH3
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Residue-Specific Description of Non-Native Transient Structures in the Ensemble of Acid-Denatured Structures of the All-β Protein c-src SH3

机译:All-β蛋白c-src SH3的酸变性结构整体中非天然瞬态结构的残基特定描述

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摘要

Secondary chemical shift analysis has been used to characterize the unfolded state of acid-ndenatured c-src SH3. Even though native c-src SH3 adopts an all-β fold, we found evidence of transientnhelicity in regions corresponding to native loops. In particular, residues 40-46, connecting the n-src loop tonthe third β-strand, exhibited an apparent helicity of nearly 45%. Furthermore, the RT loop and the divergingnturn appeared to adopt non-native-like helical conformations. Interestingly, none of the residues found inntransient helical conformations exhibited significant φ-values [Riddle, D. S., et al. (1999) Nat. Struct. Biol. 6,n1016-1024]. This indicated that the transient helicity has no influence or only a weak influence on the actualnprotein folding reaction. The residual structural propensities were compared to those of other SH3 domains,nrevealing heterogeneity in the unfolded ensemble that clearly contrasts with the conserved character of thentopology of native state and transition state ensembles typical for SH3 domains.
机译:二级化学位移分析已用于表征酸未改性的c-src SH3的未折叠状态。即使天然c-src SH3采用全β折叠,我们也发现了与天然环相对应的区域发生瞬变的证据。特别地,连接n-src环与第三条β链的残基40-46表现出近45%的表观螺旋度。此外,RT环和发散角似乎采用了非天然的螺旋构象。有趣的是,在非瞬时螺旋构象中发现的残基均未显示出显着的φ值[Riddle,D.S。,等。 (1999)Nat。结构。生物学6,n1016-1024]。这表明瞬时螺旋度对实际的蛋白折叠反应没有影响或只有很小的影响。将其余的结构倾向与其他SH3结构域进行了比较,揭示了未折叠集合中的异质性,这与SH3结构域典型的自然状态和过渡态集合的拓扑学的保守特性形成鲜明对比。

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  • 来源
    《Biochemistry》 |2010年第15期|p.3246-3253|共8页
  • 作者单位

    Structure Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5,DK-2200 Copenhagen N, Denmark;

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