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

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 con...

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Autores principales: Mizuno, Fuko, Aoki, Saeko, Matsugami, Akimasa, Hayashi, Fumiaki, Nishimura, Chiaki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Bentham Science Publishers 2023
Materias:
Life Sciences, Protein and Peptide Sciences, Biochemistry and Molecular Biology, Protein and Peptide Science
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10230605/
https://www.ncbi.nlm.nih.gov/pubmed/36600624
http://dx.doi.org/10.2174/0929866530666230104140830
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author Mizuno, Fuko
Aoki, Saeko
Matsugami, Akimasa
Hayashi, Fumiaki
Nishimura, Chiaki
author_facet Mizuno, Fuko
Aoki, Saeko
Matsugami, Akimasa
Hayashi, Fumiaki
Nishimura, Chiaki
author_sort Mizuno, Fuko
collection PubMed
description 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 C-terminal 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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spelling pubmed-102306052023-06-01 The Residual Structure of Unfolded Proteins was Elucidated from the Standard Deviation of NMR Intensity Differences Mizuno, Fuko Aoki, Saeko Matsugami, Akimasa Hayashi, Fumiaki Nishimura, Chiaki Protein Pept Lett Life Sciences, Protein and Peptide Sciences, Biochemistry and Molecular Biology, Protein and Peptide Science 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 C-terminal 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. Bentham Science Publishers 2023-02-28 2023-02-28 /pmc/articles/PMC10230605/ /pubmed/36600624 http://dx.doi.org/10.2174/0929866530666230104140830 Text en © 2023 Bentham Science Publishers https://creativecommons.org/licenses/by-nc/4.0/ This is an open access article licensed under the terms of the Creative Commons Attribution-Non-Commercial 4.0 International Public License (CC BY-NC 4.0) (https://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.
spellingShingle Life Sciences, Protein and Peptide Sciences, Biochemistry and Molecular Biology, Protein and Peptide Science
Mizuno, Fuko
Aoki, Saeko
Matsugami, Akimasa
Hayashi, Fumiaki
Nishimura, Chiaki
The Residual Structure of Unfolded Proteins was Elucidated from the Standard Deviation of NMR Intensity Differences
title The Residual Structure of Unfolded Proteins was Elucidated from the Standard Deviation of NMR Intensity Differences
title_full The Residual Structure of Unfolded Proteins was Elucidated from the Standard Deviation of NMR Intensity Differences
title_fullStr The Residual Structure of Unfolded Proteins was Elucidated from the Standard Deviation of NMR Intensity Differences
title_full_unstemmed The Residual Structure of Unfolded Proteins was Elucidated from the Standard Deviation of NMR Intensity Differences
title_short The Residual Structure of Unfolded Proteins was Elucidated from the Standard Deviation of NMR Intensity Differences
title_sort residual structure of unfolded proteins was elucidated from the standard deviation of nmr intensity differences
topic Life Sciences, Protein and Peptide Sciences, Biochemistry and Molecular Biology, Protein and Peptide Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10230605/
https://www.ncbi.nlm.nih.gov/pubmed/36600624
http://dx.doi.org/10.2174/0929866530666230104140830
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