2F4G
Triclinic cross-linked lysozyme soaked in bromoethanol 1M
2F4G の概要
| エントリーDOI | 10.2210/pdb2f4g/pdb |
| 関連するPDBエントリー | 2F2N 2F30 2F4A |
| 分子名称 | Lysozyme C, NITRATE ION, 2-BROMOETHANOL, ... (4 entities in total) |
| 機能のキーワード | denaturation, lysozyme, barnase, cross-linked crystals, glutaraldehyde, urea, thiourea, bromoethanol, 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 | 14642.14 |
| 構造登録者 | |
| 主引用文献 | Salem, M.,Mauguen, Y.,Prange, T. On the edge of the denaturation process: Application of X-ray diffraction to barnase and lysozyme cross-linked crystals with denaturants in molar concentrations. Biochim.Biophys.Acta, 1764:903-912, 2006 Cited by PubMed Abstract: Structural data about the early step of protein denaturation were obtained from cross-linked crystals for two small proteins: barnase and lysozyme. Several denaturant agents like urea, bromoethanol or thiourea were used at increasing concentrations up to a limit leading to crystal disruption (>or=2 to 6 M). Before the complete destruction of the crystal order started, specific binding sites were observed at the protein surfaces, an indication that the preliminary step of denaturation is the disproportion of intermolecular polar bonds to the benefit of the agent "parasiting" the surface. The analysis of the thermal factors first agree with a stabilization effect at low or moderate concentration of denaturants rapidly followed by a destabilization at specific weak points when the number of sites increase (overflooding effect). PubMed: 16600702DOI: 10.1016/j.bbapap.2006.02.009 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.654 Å) |
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