5B07

Lysozyme (denatured by DCl and refolded)

5B07 の概要

• エントリーDOI: 10.2210/pdb5b07/pdb
• 関連するPDBエントリー: 5B05 5B06
• 分子名称: Lysozyme C, 1,2-ETHANEDIOL, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: refolded, hydrolase
• 由来する生物種: Gallus gallus (Chicken)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14905.16

構造登録者

Kita, A.,Morimoto, Y. (登録日: 2015-10-28, 公開日: 2016-01-13, 最終更新日: 2024-10-16)

主引用文献

Kita, A.,Morimoto, Y.
An Effective Deuterium Exchange Method for Neutron Crystal Structure Analysis with Unfolding-Refolding Processes
Mol Biotechnol., 58:130-136, 2016

PubMed Abstract: A method of hydrogen/deuterium (H/D) exchange with an unfolding-refolding process has been applied to hen egg-white lysozyme (HWL), and accurate evaluation of its deuteration was carried out by time-of-flight mass spectroscopy. Neutron crystallography requires a suitable crystal with enough deuterium exchanged in the protein to decrease incoherent scattering from hydrogens. It is very expensive to prepare a fully deuterated protein, and therefore a simple H/D exchange technique is desirable for this purpose. Acid or base addition to protein solutions with heating effectively increased the number of deuterium up to more than 20 % of that of all hydrogen atoms, and refolded structures were determined by X-ray structure analysis at 1.8 Å resolution. Refolded HWL had increased deuterium content in its protein core and its native structure, determined at atomic resolution, was fully preserved.

PubMed: 26718545
DOI: 10.1007/s12033-015-9908-8

実験手法

X-RAY DIFFRACTION (1.8 Å)