Structure, Dynamics, and Solvent in Crambin Crystals at 1A Resolution

这个项目的目标是在原子分辨率下获得蛋白质及其溶剂环境的图像，并测试分子动力学和蛋白质运动的正常模式处理对结构中原子迁移率的模拟情况。这些研究的测试系统是有序、疏水的蛋白质Crambin，它的衍射至少为0.83A。潜在的动机是通过确定蛋白质的平衡几何和振动运动，并通过经验势能函数计算晶体中的相互作用力的大小，来了解稳定蛋白质折叠的力。Crambin提供了一个独特的机会，以真正的原子分辨率查看蛋白质及其周围的溶剂，不受限制蛋白质模型的影响。这些信息有很多好处。对于蛋白质本身，可以看到多肽单元的几何形状。可以检测蛋白质内和水中的氢键距离和角分布。水分子在蛋白质表面的极性基团和非极性基团周围的排列可能为在其他蛋白质表面周围构建水和理解酶活性部位的水提供了一个模型。

The goals of this project are to obtain a picture of a protein and its solvent environment at atomic resolution and to test how well the mobility of atoms in the structure is modeled by molecular dynamics and normal mode treatments of protein motion. The test system for these studies is the well-ordered, hydrophobic protein, crambin, which diffracts to at least 0.83 A. An underlying motivation is to understand the forces which stabilize protein folding by determination of the protein's equilibrium geometry and vibrational motion and by calculating the magnitude of the interaction forces in the crystal with an empirical potential energy function. Crambin presents a unique opportunity to view a protein with its surrounding solvent at truly atomic resolution, unprejudiced by a restraining protein model. There are numerous benefits from this information. The geometry of the peptide unit can be seen for the protein itself. The hydrogen bonding distances and angular distributions both within the protein and for the water can be examined. The arrangement of water molecules around polar and nonpolar groups at the protein surface may provide a model for building water around other protein surfaces and for understanding water at the active sites of enzymes.