Magnetic Resonance
Magnetic Resonance
MR
Articles | Volume 2, issue 1
Articles | Volume 2, issue 1
https://doi.org/10.5194/mr-2-223-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
Special issue:
https://doi.org/10.5194/mr-2-223-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
Articles | Volume 2, issue 1
Research article
 | 
26 Apr 2021
Research article |  | 26 Apr 2021

Conformational features and ionization states of Lys side chains in a protein studied using the stereo-array isotope labeling (SAIL) method

Mitsuhiro Takeda, Yohei Miyanoiri, Tsutomu Terauchi, and Masatsune Kainosho

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Latest update: 21 Nov 2024
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Short summary
Although both the hydrophobic aliphatic chain and hydrophilic ζ-amino group of the lysine side chain presumably contribute to the structures and functions of proteins, the dual nature of the lysine residue has not been fully understood yet, due to the lack of appropriate methods to acquire comprehensive information on its long consecutive methylene chain at the atomic scale. We describe herein a novel strategy to address the current situation using nuclear magnetic resonance spectroscopy.
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