MULTI-CONFORMATIONAL PEPTIDE DYNAMICS DERIVED FROM NMR DATA A NEW SEARCH ALGORITHM AND ITS APPLICATION TO ANTAMANIDE
MULTI-CONFORMATIONAL PEPTIDE DYNAMICS DERIVED FROM NMR DATA A NEW SEARCH ALGORITHM AND ITS APPLICATION TO ANTAMANIDE
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DOI：
10.1007/bf01874565
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发表时间：
1991-01-01
影响因子：
2.7
通讯作者：
ERNST R R
中科院分区：
文献类型：
--
作者：
BRUSCHWEILER R;BLACKLEDGE M;ERNST R R
提出了一种称为 MEDUSA 的搜索算法，该算法允许根据实验高分辨率 NMR 数据确定溶液中生物分子的多种构象，交换率常数通常在 103 至 107 s-1 之间。生成的多个结构与 NMR 交叉弛豫率（NOESY、ROESY）、标量 J 耦合常数和 T1.rho 一致。测量。该算法应用于溶解在氯仿中的环状十肽antamanid。 T1.rho 的特征射频场依赖性。 Val1 和 Phe6 的 NH 质子的弛豫率可以通过两个结构之间的动态交换来解释。
A search algorithm, called MEDUSA, is presented which allows the determination of multiple conformations of biomolecules in solution with exchange rate constants typically between 103 and 107 s-1 on the basis of experimental high-resolution NMR data. Multiples of structures are generated which are consistent as ensembles with NMR cross-relaxation rates (NOESY, ROESY), scalar J-coupling constants, and T1.rho. measurements. The algorithm is applied to the cyclic decapeptide antamanide dissolved in chloroform. The characteristic radio-frequency field dependence of the T1.rho. relaxation rates found for the NH protons of Val1 and Phe6 can be explained by a dynamical exchange between two structures.