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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Folding pathways of proteins with increasing degree of sequence identities but different structure and function
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Folding pathways of proteins with increasing degree of sequence identities but different structure and function

机译：具有更高序列同一性但结构和功能不同的蛋白质的折叠途径

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摘要

Much experimental work has been devoted in comparing the folding behavior of proteins sharing the same fold but different sequence. The recent design of proteins displaying very high sequence identities but different 3D structure allows the unique opportunity to address the protein-folding problem from a complementary perspective. Here we explored by Φ-value analysis the pathways of folding of three different heteromorphic pairs, displaying increasingly high-sequence identity (namely, 30%, 77%, and 88%), but different structures called G_A (a 3-α helix fold) and G_B (an α/β fold). The analysis, based on 132 site-directed mutants, is fully consistent with the idea that protein topology is committed very early along the pathway of folding. Furthermore, data reveals that when folding approaches a perfect two-state scenario, as in the case of the G_A domains, the structural features of the transition state appear very robust to changes in sequence composition. On the other hand, when folding is more complex and multistate, as for the GBs, there are alternative nuclei or accessible pathways that can be alternatively stabilized by altering the primary structure. The implications of our results in the light of previous work on the folding of different members belonging to the same protein family are discussed.
机译：在比较具有相同折叠但不同序列的蛋白质的折叠行为方面，已经进行了大量实验工作。蛋白质的最新设计显示出很高的序列同一性，但具有不同的3D结构，这为从互补的角度解决蛋白质折叠问题提供了独特的机会。在这里，我们通过Φ值分析探索了三个不同的异形对的折叠路径，显示出越来越高的序列同一性（即30％，77％和88％），但是不同的结构称为G_A（3-α螺旋折叠） ）和G_B（α/β折叠）。该分析基于132个定点突变体，完全符合蛋白质拓扑在折叠路径早期就完成的想法。此外，数据表明，当折叠接近完美的两态情况时，例如在G_A域的情况下，过渡态的结构特征似乎对序列组成的变化非常稳健。另一方面，当折叠更复杂且处于多态时，就GB而言，存在其他原子核或可及途径，可以通过改变一级结构来使其稳定。讨论了根据先前工作对属于同一蛋白质家族的不同成员折叠的研究结果的含义。

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  • 作者

    Rajanish Giri; Angela Morrone; Carlo Travaglini-Allocatelli; Per Jemth; Maurizio Brunori; Stefano Gianni;

  • 作者单位

    Istituto Pasteur-Fondazione Cenci Bolognetti, Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli,' Universita di Roma 'La Sapienza,' Piazzale A. Moro 5, 00185 Rome, Italy;

    Istituto Pasteur-Fondazione Cenci Bolognetti, Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli,' Universita di Roma 'La Sapienza,' Piazzale A. Moro 5, 00185 Rome, Italy;

    Istituto Pasteur-Fondazione Cenci Bolognetti, Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli,' Universita di Roma 'La Sapienza,' Piazzale A. Moro 5, 00185 Rome, Italy;

    Department of Medical Biochemistry and Microbiology, Uppsala University, Biomedical Center Box 582, SE-75123 Uppsala, Sweden;

    Istituto Pasteur-Fondazione Cenci Bolognetti, Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli,' Universita di Roma 'La Sapienza,' Piazzale A. Moro 5, 00185 Rome, Italy,Department of Medical Biochemistry and Microbiology, Uppsala University, Biomedical Center Box 582, SE-75123 Uppsala, Sweden;

    Istituto Pasteur-Fondazione Cenci Bolognetti, Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli,' Universita di Roma 'La Sapienza,' Piazzale A. Moro 5, 00185 Rome, Italy;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    kinetics; protein engineering; protein folding; protein G;

    机译：动力学;蛋白质工程;蛋白质折叠蛋白G;

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