Abstract
In recent years, interfacial mobility has gained popularity as a model with which to rationalize both affinity in ligand binding and the often observed phenomenon of enthalpy-entropy compensation. While protein contraction and reduced mobility, as demonstrated by computational and NMR techniques respectively, have been correlated to entropies of binding for a variety of systems, to our knowledge, Raman difference spectroscopy has never been included in these analyses. Here, nonresonance Raman difference spectroscopy, isothermal titration calorimetry, and X-ray crystallography were utilized to correlate protein contraction, as demonstrated by an increase in protein interior packing and decreased residual protein movement, with trends of enthalpy-entropy compensation. These results are in accord with the interfacial mobility model and lend additional credence to this view of protein activity.
Original language | English |
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Pages (from-to) | 11515-11523 |
Number of pages | 9 |
Journal | Journal of the American Chemical Society |
Volume | 133 |
Issue number | 30 |
DOIs | |
Publication status | Published - 3 Aug 2011 |
Keywords
- STROMELYSIN CATALYTIC DOMAIN
- X-RAY-STRUCTURE
- MATRIX-METALLOPROTEINASE INHIBITORS
- RAMAN DIFFERENCE SPECTROSCOPY
- TRYPTOPHAN SIDE-CHAINS
- LIGAND-BINDING ENERGY
- CARBONIC-ANHYDRASE-II
- PROTEIN-STRUCTURE
- SOLVENT REORGANIZATION
- CONFORMATIONAL ENTROPY