Abstract
Ribonuclease T1 (RNase T1)(EC.3.1.27.3) from Aspergillus oryzae specifically cleaves single-stranded RNA on the 3’ side of guanylic acid residues (1). Recently, the three dimensional structure of RNase T1 has been determined by X-ray crystallographic work in the presence of 2’GMP (2,3) and 3’GMP (4). The available structural information, its specific recognition of guanosine bases and being relatively small (M.W. 11,085) make RNase T1 a good model system for the study of the interaction between proteins and nucleic acids.
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© 1987 Springer-Verlag Berlin Heidelberg
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MacKerell, A.D., Rigler, R., Hahn, U., Saenger, W. (1987). Ribonuclease T1: Interaction with 2’GMP and 3’GMP as Studied by Time-Resolved Fluorescence Spectroscopy. In: Ehrenberg, A., Rigler, R., Gräslund, A., Nilsson, L. (eds) Structure, Dynamics and Function of Biomolecules. Springer Series in Biophysics, vol 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71705-5_55
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DOI: https://doi.org/10.1007/978-3-642-71705-5_55
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