7FGU

H/D exchanged Hen egg-white lysozyme denatured in basic conditions and refolded in solution

7FGU の概要

• エントリーDOI: 10.2210/pdb7fgu/pdb
• 関連するPDBエントリー: 7FG8 7FGV
• 分子名称: Lysozyme C, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: h/d exchange, denatured and refolded, hydrolase
• 由来する生物種: Gallus gallus (Chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14389.60

構造登録者

Kita, A.,Morimoto, Y. (登録日: 2021-07-28, 公開日: 2022-02-09, 最終更新日: 2024-11-06)

主引用文献

Kita, A.,Morimoto, Y.
Hydrogen/Deuterium Exchange Behavior During Denaturing/Refolding Processes Determined in Tetragonal Hen Egg-White Lysozyme Crystals.
Mol Biotechnol., 64:590-597, 2022

PubMed Abstract: The hydrogen/deuterium (H/D) exchange of main-chain amide hydrogens in the protein that denatured and refolded in deuterated solvent is considered to contain the traces of hydrogen bond cleavages or the exposure to solvent of the buried part of the protein during the denaturing and refolding (denaturing/refolding) processes. Here, we report the H/D exchange behaviors in hen egg-white lysozymes denatured under acidic conditions, basic conditions, and thermal conditions and then refolded in deuterated solvents, using crystallographic methods. The results indicate that the space containing the Trp28 side chain was hardly exposed to the solvent in acidic conditions, but exposed under basic or heated conditions. Moreover, the β-bridges between Tyr53 and Ile58 in strands β2 and β3, which are in a highly conserved region, show some tolerance to changes in pD. The results indicate that crystallographic method is one of the powerful tools to analyze the denaturing/refolding processes of proteins.

PubMed: 35028904
DOI: 10.1007/s12033-022-00447-7

実験手法

NEUTRON DIFFRACTION (2.3 Å)
X-RAY DIFFRACTION (2 Å)