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Updated: May 3, 2026

A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing
11:36

A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing

Published on: July 3, 2016

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NMR誘導変異を用いたタンパク質の液体-液体相分離を調節するためのプロトコル

Mayu Enomoto-Kusano1, Kyoko Furuita2,3, Takashi S Kodama2

  • 1Graduate School of Engineering Science, Yokohama National University, Tokiwadai 79-5, Hodogaya-ku, Yokohama 240-8501, Kanagawa, Japan.

Methods and protocols
|February 20, 2026
PubMed
まとめ

研究者は,タンパク質構造と液体液相分離 (LLPS) を結びつける新しい方法を開発しました. このテクニックは,核磁共鳴 (NMR) と突然変異を用いてタンパク質の振る舞いを制御し,細胞区画形成の洞察を提供します.

キーワード:
NMRによる誘導性変異遺伝.VAPBは,VAPBと一致している.液体液体相分離装置核磁気共鳴による核磁気共鳴は,タンパク質コンデンサートは,タンパク質のダイナミクス

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¹H NMR: Complex Splitting

A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
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¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

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In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
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Spin decoupling is usually achieved by...
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