Structural Biology Research Center, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan
Department of Structural BioImaging, Faculty of Life Sciences, Kumamoto University, 5-1, Oe-honmachi, Chuo-ku, Kumamoto, 862-0973, Japan
Yohei Miyanoiri
Structural Biology Research Center, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan
Research Center for State-of-the-Art Functional Protein Analysis, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan
Tsutomu Terauchi
SAIL Technologies Co., Inc., 2008-2 Wada, Tama-city, Tokyo, 206-0001, Japan
Graduate School of Science, Tokyo Metropolitan University, 1-1
Minami-ohsawa, Hachioji, Tokyo, 192-0397, Japan
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.
Although both the hydrophobic aliphatic chain and hydrophilic ζ-amino group of the lysine side...
