The Residual Structure of Unfolded Proteins was Elucidated from the Standard Deviation of NMR Intensity Differences.

IF 1 4区生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY

Protein and Peptide Letters Pub Date : 2023-01-01 DOI:10.2174/0929866530666230104140830

Fuko Mizuno, Saeko Aoki, Akimasa Matsugami, Fumiaki Hayashi, Chiaki Nishimura

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Abstract

Introduction: Sensitive methods are necessary to identify the residual structure in an unfolded protein, which may be similar to the functionally native structure. Signal intensity in NMR experiments is useful for analyzing the line width for a dynamic structure; however, another contribution is contained.

Methods: Here, the signal-intensity difference along the sequence was used for probability to calculate the standard deviation.

Results: The relative values of the standard deviations were 0.57, 0.57, and 0.66 for alpha-synuclein wild-type, A53T, and A30P, respectively. This revealed that the flexible region was mainly in the Cterminal region of alpha-synuclein at higher temperatures as observed by the amide-proton exchange studies.

Conclusion: In particular, the flexible structure was induced by the A30P mutation.

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利用核磁共振强度差的标准差分析了未折叠蛋白的残馀结构。

未折叠蛋白中的残馀结构可能与功能上的天然结构相似，因此有必要采用敏感的方法来鉴定残馀结构。核磁共振实验中的信号强度可用于分析动态结构的线宽;然而，它包含了另一个贡献。方法:采用沿序列的信号强度差作为概率计算标准偏差。结果α -synuclein野生型、A53T和A30P的相对标准差分别为0.57、0.57和0.66。这表明，在较高的温度下，柔性区主要在α -突触核蛋白的c端区域，这是由酰胺-质子交换研究观察到的。结论:特别是A30P突变诱导了柔性结构。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Protein and Peptide Letters 生物-生化与分子生物学

CiteScore

2.90

自引率

0.00%

发文量

审稿时长

2 months

期刊介绍： Protein & Peptide Letters publishes letters, original research papers, mini-reviews and guest edited issues in all important aspects of protein and peptide research, including structural studies, advances in recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, and drug design. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallization and preliminary structure determination of biologically important proteins are considered only if they include significant new approaches or deal with proteins of immediate importance, and preliminary structure determinations of biologically important proteins. Purely theoretical/review papers should provide new insight into the principles of protein/peptide structure and function. Manuscripts describing computational work should include some experimental data to provide confirmation of the results of calculations. Protein & Peptide Letters focuses on: Structure Studies Advances in Recombinant Expression Drug Design Chemical Synthesis Function Pharmacology Enzymology Conformational Analysis Immunology Biotechnology Protein Engineering Protein Folding Sequencing Molecular Recognition Purification and Analysis