作者: Zhongyu Yang , Ming Ji , Timothy F. Cunningham , Sunil Saxena
DOI: 10.1016/BS.MIE.2015.05.026
关键词:
摘要: Electron spin resonance (ESR) spectroscopy in combination with site-directed labeling has been widely used to determine the structure and dynamics of proteins other biomolecules. The most popular label is a nitroxide-based radical which can be attached protein via site-specific reaction either native cysteines or engineered into system mutagenesis. Paramagnetic transition metals, including Cu(2+), often serve as cofactors metalloproteins, have already realized ESR probes report structural information these proteins. This chapter summarizes recent methodological development from our laboratory utilizing Cu(2+) an probe distance information. We focus on detailed experimental procedures, optimized instrumental parameters, data analysis approaches order guide one who new field. Theory applications metal reviewed literature are not this chapter. A few examples methods listed end.