Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8679422 | Thrombosis Research | 2018 | 7 Pages |
Abstract
Exosite 2-induced conformational change in thrombin's active site is strongly dependent on the structure of the ligand, which has consequences with respect to regulation of thrombin. The ionic and non-ionic contributions to binding affinity and the thermodynamic signature were highly ligand specific. Interestingly, LMWLs display preference for the sodium-bound form of thrombin, which supports the existence of an energetic coupling between exosite 2 and sodium-binding site of thrombin.
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Authors
May H. Abdel Aziz, Umesh R. Desai,