Harvey T S, Wilkinson A J, Tappin M J, Cooke R M, Campbell I D
Department of Biochemistry, University of Oxford, England.
Eur J Biochem. 1991 Jun 15;198(3):555-62. doi: 10.1111/j.1432-1033.1991.tb16050.x.
The solution structure of transforming growth factor alpha has been determined by a combination of high-resolution 1H-nuclear magnetic resonance and distance geometry and restrained molecular dynamics. The 382 restraints derived from the NMR experiments were used to calculate many distance geometry structures, which were then refined by restrained molecular mechanics. Five of these structures were further refined using a variety of methods. Comparison of independently measured parameters, such as calculated hydrogen bonding patterns and experimental amide exchange rates, have been used to evaluate the accuracy of the structures. Also, possible mechanisms to explain the pH-dependent conformational interconversion observed are suggested. Finally comparisons between this work and others on this topic have been made.
转化生长因子α的溶液结构已通过高分辨率1H核磁共振、距离几何和受限分子动力学相结合的方法确定。源自核磁共振实验的382个约束条件用于计算许多距离几何结构，然后通过受限分子力学进行优化。其中五个结构使用多种方法进一步优化。通过比较独立测量的参数，如计算出的氢键模式和实验酰胺交换率，来评估结构的准确性。此外，还提出了解释观察到的pH依赖性构象相互转化的可能机制。最后，将这项工作与该主题的其他研究进行了比较。
