EPJ Web of Conferences 41, 06008 (2013)
https://doi.org/10.1051/epjconf/20134106008
https://doi.org/10.1051/epjconf/20134106008
Hydrophobic hydration of globular proteins studied with 2D-IR spectroscopy
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA
Ultrafast 2D-IR spectroscopy of a CO ligand bound to a copper active site of an artificial metalloenzyme is used as a sensitive probe of both the flexibility and the electrostatic environment of the engineered catalyst.
© Owned by the authors, published by EDP Sciences, 2013
This is an Open Access article distributed under the terms of the Creative Commons Attribution License 2.0, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
