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2HEA

CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

2HEA の概要
エントリーDOI10.2210/pdb2hea/pdb
分子名称LYSOZYME, SODIUM ION (3 entities in total)
機能のキーワードhydrolase, o-glycosyl, glycosidase
由来する生物種Homo sapiens (human)
細胞内の位置Secreted: P61626
タンパク質・核酸の鎖数1
化学式量合計14701.60
構造登録者
Takano, K.,Funahashi, J.,Yamagata, Y.,Fujii, S.,Yutani, K. (登録日: 1997-09-16, 公開日: 1998-01-14, 最終更新日: 2024-10-30)
主引用文献Takano, K.,Funahashi, J.,Yamagata, Y.,Fujii, S.,Yutani, K.
Contribution of water molecules in the interior of a protein to the conformational stability.
J.Mol.Biol., 274:132-142, 1997
Cited by
PubMed Abstract: Water molecules frequently occur in the interior of globular proteins. To elucidate the contribution of buried water molecules to the conformational stability of a protein, we examined the crystal structures and the thermodynamic parameters of denaturation of six Ile to Ala/Gly mutant human lysozymes, in which a cavity is created at each mutation site by the substitution of a smaller side-chain for a larger one. One or two ordered water molecules were found in the cavities created in some mutants (I106A, I59A and I59G). The cavity volumes for these three mutants were bigger than those that remained empty in the other mutants. The stability of the mutant proteins with the newly introduced water molecules was about 8 kJ/mol higher than that expected from the change in hydrophobic surface area (DeltaDeltaASAHP) exposed upon denaturation. It was concluded that a water molecule in a cavity created in the interior of a protein contributes favorably to the stability.
PubMed: 9398521
DOI: 10.1006/jmbi.1997.1365
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 2hea
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-12-18に公開中

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