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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Differences in the folding transition state of ubiquitin indicated by phi and psi analyses.
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Differences in the folding transition state of ubiquitin indicated by phi and psi analyses.

机译：phi和psi分析表明泛素的折叠过渡状态存在差异。

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摘要

We compare the folding transition state (TS) of ubiquitin previously identified by using psi analysis to that determined by using analysis. Both methods attempt to identify interactions and their relative populations at the rate-limiting step for folding. The TS ensemble derived from psi analysis has an extensive native-like chain topology, with a four-stranded beta-sheet network and a portion of the major helix. According to analysis, however, the TS is much smaller and more polarized, with only a local helix/hairpin motif. We find that structured regions can have values far from unity, the canonical value for such sites, because of structural relaxation of the TS. Consequently, these sites may be incorrectly interpreted as contributing little to the structure of the TS. These results stress the need for caution when interpreting and drawing conclusions from analysis alone and highlight the need for more specific tools for examining the structure and energetics of the TS ensemble.
机译：我们将先前使用psi分析确定的泛素的折叠过渡状态（TS）与使用分析确定的折叠过渡状态进行比较。两种方法都试图在折叠的限速步骤中识别相互作用及其相对种群。源自psi分析的TS合奏具有广泛的类似于本机的链拓扑，具有四链β-折叠网络和部分主要螺旋。然而，根据分析，TS较小且极化更多，只有局部螺旋/发夹基序。我们发现，由于TS的结构松弛，结构化区域的值可能远非统一，即此类站点的标准值。因此，这些位点可能被错误地解释为对TS结构的贡献很小。这些结果强调仅在解释和得出分析结论时需要谨慎，并强调需要使用更具体的工具来检查TS集成的结构和能量学。

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