Hsu Shang-Te Danny, Dobson Christopher M
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Biomol NMR Assign. 2009 Jun;3(1):17-20. doi: 10.1007/s12104-008-9130-8. Epub 2008 Nov 18.
Trigger factor (TF) is a multi-domain molecular chaperone that binds to the bacterial ribosome at the tunnel exit from which nascent polypeptides emerge. We present here the NMR assignments of the ribosome binding domain (RBD) of TF from Escherichia coli as a stable 26 kDa dimer, using conditions that are similar to a crystallographic study from which an X-ray crystal structure of the identical construct was determined.
触发因子（TF）是一种多结构域分子伴侣，它在新生多肽出现的通道出口处与细菌核糖体结合。我们在此展示了来自大肠杆菌的TF核糖体结合结构域（RBD）作为稳定的26 kDa二聚体的核磁共振（NMR）归属，所使用的条件类似于一项晶体学研究，该研究确定了相同构建体的X射线晶体结构。
