PKAS OF RESIDUES IN PROTEINS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 可电离残基占蛋白质残基的25%。电离的原位能量学决定了残基可以发挥什么功能作用。酸或碱催化剂需要接近生理pH的pKAs才能成为良好的质子供体或受体。质子转移需要连接残基，在那里质子化和去质子化状态是热可及的。类似的pKA残基簇可以形成内部缓冲区，因此质子可以随着反应的进行而移动。MCCE提供了一种一致地计算和比较不同蛋白质中的pKas的方法。所需的计算机时间将用于计算500种不同蛋白质的pKA。将对这些进行分析，以确定蛋白质如何与电荷相互作用。结果将被添加到一个可搜索的数据库中，该数据库包含35,000个计算的pKA(www.sor.ccny.cuny.edu/~mcce)。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Ionizable residues make up 25% of the residues in proteins. The in situ energetics of ionization determines what functional roles residues can play. Acid or base catalysts need pKas near physiological pH to be good proton donors or acceptors. Proton transfers need connecting residues where protonated and deprotonated states are thermally accessible. Clusters of residues of similar pKas can form internal buffers so protons can move as reactions progress. MCCE provides a way to consistently calculate and compare pKas in different proteins. The requested computer time will be used to calculate pKas for 500 disparate proteins. These will be analyzed to determine how proteins interact with charges. The results will be added to a searchable database of 35,000 calculated pKas (www.sci.ccny.cuny.edu/~mcce).