CRYSTALLOGRAPHIC STUDIES OF MOLECULAR CHAPERONES

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。 我们正在继续研究分子伴侣蛋白的结构和机制，广泛地说，这有助于蛋白质和RNA分子在细胞中正确的折叠、组装和靶向。目前正在研究的系统包括“原核蛋白酶体”--一个850 kDa的复合体，它是真核蛋白酶体的简单同系物；一个促进细菌中膜蛋白折叠和组装的伴侣；以及一个调节细胞中RNA结构的RNA伴侣/解旋酶家族。结合其他生物物理研究，我们现在正在通过表征靶标多肽或RNA和共结晶络合物来确定结构，从而检查其中许多蛋白质的底物识别特性。

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. We are continuing our studies on the structure and mechanism of molecular chaperone proteins which, broadly speaking, facilitate the correct folding, assembly and targeting of proteins and RNA molecules in cells. Systems that are currently under study include a "prokaryotic proteasome"?a 850 kDa complex that is a simple homolog of the eukaryotic proteasome; a chaperone that facilitates folding and assembly of membrane proteins in bacteria; and a family of RNA chaperones/helicases that modulate RNA structure in cells. Combined with other biophysical studies, we are now examining substrate recognition properties of many of these proteins by characterizing target peptides or RNAs and co-crystallizing complexes for structure determination.