STRUCTURE-DERIVED HYDROPHOBIC POTENTIAL - HYDROPHOBIC POTENTIAL DERIVED FROM X-RAY STRUCTURES OF GLOBULAR-PROTEINS IS ABLE TO IDENTIFY NATIVE FOLDS
STRUCTURE-DERIVED HYDROPHOBIC POTENTIAL - HYDROPHOBIC POTENTIAL DERIVED FROM X-RAY STRUCTURES OF GLOBULAR-PROTEINS IS ABLE TO IDENTIFY NATIVE FOLDS
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DOI：
10.1016/0022-2836(92)90556-y
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发表时间：
1992-04-05
影响因子：
5.6
通讯作者：
SIPPL, MJ
中科院分区：
文献类型：
--
作者：
CASARI, G;SIPPL, MJ
我们提出了一个模型，在球状蛋白质的疏水相互作用，这是完全基于已知的X-射线结构的分析。这种结构衍生的疏水力被认为是稳定天然折叠的非共价相互作用中最强的。发现疏水性相互作用的函数形式是线性的，对应于沿着可观察距离范围（5至70 Å）的恒定力。疏水性氨基酸对电位的参数产生的结构衍生的疏水性规模，强烈相关的规模由各种互补的方法。我们证明，结构衍生的疏水相互作用单独是能够区分大量的天然构象从一个大的错误折叠的结构池。
We present a model for the hydrophobic interaction in globular proteins that is based entirely on an analysis of known X-ray structures. This structure-derived hydrophobic force is identified as the strongest among the non-covalent interactions that stabilize native folds. The functional form of the hydrophobic interaction is found to be linear, corresponding to a constant force along the observable distance range (5 to 70 Å). The parameters of the hydrophobic amino acid pair potentials yield a structure-derived hydrophobicity scale that correlates strongly with scales derived by a variety of complementary approaches. We demonstrate that the structure-derived hydrophobic interaction alone is able to distinguish a substantial number of native conformations from a large pool of misfolded structures.