Publikationsserver
The well-tempered Thrombin - A systematic crystallographic and calorimetric study on the thermodynamics of serine-protease inhibition
The presented study contributes to the fundamental understanding of molecular recognition of small molecules by a macromolecular host protein. The biophysical properties of a large set of systematically varied thrombin inhibitors were anatomized in detail. In particular the combination of structural...
Tallennettuna:
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| Muut tekijät: | |
| Aineistotyyppi: | Dissertation |
| Kieli: | englanti |
| Julkaistu: |
Philipps-Universität Marburg
2009
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| Aiheet: | |
| Linkit: | PDF-kokoteksti |
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| Yhteenveto: | The presented study contributes to the fundamental understanding of molecular recognition of small molecules by a macromolecular host protein. The biophysical properties of a large set of systematically varied thrombin inhibitors were anatomized in detail. In particular the combination of structural information from X-ray crystallography with thermodynamic data from microcalorimetry allowed following the thermodynamically relevant differences resulting in the binding process. The approach of systematically varying biophysical properties of protein inhibitors in small steps permits conclusive statements on the contribution of individual functionalities to binding affinity, as the outstanding complexity of the binding thermodynamics could be reduced to the comparison of closely related inhibitors. Reorganization of solute molecules was explicitly considered in all discussions of the factors determining the widely varying binding affinity of the inhibitors to their target. |
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| Ulkoasu: | 152 Seiten |
| DOI: | 10.17192/z2009.0698 |