Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains.

Abstract

Calmodulin is a two-domain protein which in solution can adopt a variety of conformations upon reorientation of its domains. The maximum occurrence (MO) of a set of calmodulin conformations that are representative of the overall conformational space possibly sampled by the protein, has been calculated from the paramagnetism-based restraints. These restraints were measured after inclusion of a lanthanide binding tag in the C-terminal domain to supplement the data obtained by substitution of three paramagnetic lanthanide ions to the calcium ion in the second calcium binding loop of the N-terminal domain. The analysis shows that the availability of paramagnetic restraints arising from metal ions placed on both domains, reduces the MO of the conformations to different extents, thereby helping to identify those conformations that can be mostly sampled by the protein.

DOI: 10.1007/s10858-011-9532-2

Cite this paper

@article{Dasgupta2011NarrowingTC, title={Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains.}, author={Soumyasri Dasgupta and Xiaoyu Hu and Peter H J Keizers and Wei-Min Liu and Claudio Luchinat and Malini Nagulapalli and Mark Overhand and Giacomo Parigi and Luca Sgheri and Marcellus Ubbink}, journal={Journal of biomolecular NMR}, year={2011}, volume={51 3}, pages={253-63} }