Articles | Volume 2, issue 1
https://doi.org/10.5194/mr-2-223-2021
https://doi.org/10.5194/mr-2-223-2021
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

Viewed

Total article views: 1,452 (including HTML, PDF, and XML)
HTML PDF XML Total BibTeX EndNote
815 586 51 1,452 31 27
  • HTML: 815
  • PDF: 586
  • XML: 51
  • Total: 1,452
  • BibTeX: 31
  • EndNote: 27
Views and downloads (calculated since 19 Feb 2021)
Cumulative views and downloads (calculated since 19 Feb 2021)

Viewed (geographical distribution)

Total article views: 1,452 (including HTML, PDF, and XML) Thereof 1,332 with geography defined and 120 with unknown origin.
Country # Views %
  • 1
1
 
 
 
 
Latest update: 21 Feb 2024
Download
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.