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

这个项目的目标是获得一个蛋白质的图片 和它的溶剂环境在原子分辨率和测试如何 结构中原子的迁移率由 分子动力学和蛋白质运动的正常模式处理。 这些研究的测试系统是有序的， 疏水蛋白，crambin，其衍射至至少0.83 A。 一个潜在的动机是理解 通过测定蛋白质的 平衡几何和振动运动， 晶体中的相互作用力的大小， 经验势能函数 Crambin提供了一个独特的机会，以查看蛋白质与其 周围的溶剂在真正的原子分辨率，不受影响， 抑制蛋白质模型 有许多好处， 的该项目海外 可以看到肽单元的几何形状 蛋白质本身。 氢键距离和 蛋白质和水的角分布 可以检查。 水分子在两极周围的排列 蛋白质表面的非极性基团可以提供一个模型 在其他蛋白质表面构建水， 了解酶活性部位的水。

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.