RNase H 15N relaxation study

Dynamics of Escherichia coli Ribonuclease H

Backbone Dynamics of Escherichia coli Ribonuclease HI: Correlations with Structure and Function in an Active Enzyme

Mandel, A.M., Akke, M., & Palmer, A.G. (1995) J. Mol. Biol. 246, 144-163.

Dynamics of ribonuclease H: Temperature dependence of motions on multiple time scales

Mandel, A.M, Akke, M., & Palmer, A.G. (1996) Biochemistry 35, 16009-16023.

Longitudinal and transverse ¹H - ¹⁵N dipolar/¹⁵N chemical shift anisotropy relaxation interference: Unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules

C. D. Kroenke, J. P. Loria, L. K. Lee, M. Rance and A. G. Palmer J. Am. Chem. Soc. 120, 7905-7915 (1998).

Variability of the ¹⁵N chemical shift anisotropy in Escherichia coli ribonuclease H in solution

C. D. Kroenke, M. Rance and A. G. Palmer J. Am. Chem. Soc. 121, 10119-10125 (1999).

The ¹⁵N order parameters are color coded (yellow corresponds to low order parameters, violet to high) onto the crystal structure 1rnh, solved by Yang and coworkers in the Hendrickson lab here at Columbia University.

Hierarchical links

Last modified 7/25/02 Kemal Eren. Send comments to agp6@columbia.edu