4HB1
A DESIGNED FOUR HELIX BUNDLE PROTEIN.
4HB1 の概要
| エントリーDOI | 10.2210/pdb4hb1/pdb |
| 分子名称 | DHP1, UNKNOWN ATOM OR ION (3 entities in total) |
| 機能のキーワード | designed helical bundle |
| 由来する生物種 | synthetic construct |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 11815.36 |
| 構造登録者 | Schafmeister, C.E.,Laporte, S.L.,Miercke, L.J.W.,Stroud, R.M. (登録日: 1997-11-10, 公開日: 1998-03-04, 最終更新日: 2024-04-03) |
| 主引用文献 | Schafmeister, C.E.,LaPorte, S.L.,Miercke, L.J.,Stroud, R.M. A designed four helix bundle protein with native-like structure. Nat.Struct.Biol., 4:1039-1046, 1997 Cited by PubMed Abstract: A 108 amino acid protein was designed and constructed from a reduced alphabet of seven amino acids. The 2.9 A resolution X-ray crystal structure confirms that the protein is a four helix bundle, as it was designed to be. Hydrogen/deuterium exchange experiments reveal buried amide protons with protection factors in excess of 1 x 10(6) in the range characteristic of well protected protons in functional folded proteins (10(3)-10(8)) rather than protons in rapid exchange (0-10(2)). The protein is monomeric at 1 mM, the concentration at which the exchange experiments were undertaken, indicating that the exchange factors are due to a unique stable tertiary structure fold, and not due to any higher order quaternary structure. Thermodynamic analysis provides an estimate of the free energy of folding of -9.3 kcal mole-1 at 25 degrees C, consistent with the free energy of folding derived from the protection factors of the most protected protons, indicating that global unfolding is required for exchange of the most protected protons. PubMed: 9406555DOI: 10.1038/nsb1297-1039 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.9 Å) |
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