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


Interactive discussion

Status: closed

Comment types: AC – author | RC – referee | CC – community | EC – editor | CEC – chief editor | : Report abuse
  • RC1: 'Comment on mr-2021-15', Anonymous Referee #1, 25 Feb 2021
  • RC2: 'Comment on mr-2021-15', Anonymous Referee #2, 25 Feb 2021
  • RC3: 'Comment on mr-2021-15', Anonymous Referee #3, 04 Mar 2021

Peer review completion

AR: Author's response | RR: Referee report | ED: Editor decision
AR by Masatsune Kainosho on behalf of the Authors (31 Mar 2021)  Author's response    Author's tracked changes    Manuscript
ED: Publish as is (13 Apr 2021) by Rolf Boelens
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.