Thermodynamic consequences of disrupting a water‐mediated hydrogen bond network in a protein:pheromone complex

By Scott D. Sharrow, K. Edmonds, M. A. Goodman, M. Novotny, M. Stone. 2005

38 citations recorded by the source corpus.

Subfields: Computational Theory and Mathematics, Organic Chemistry, Physical and Theoretical Chemistry

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

1. S. Perez-Miller
2. T. Pertinhez
3. Q. Zou
4. M. Novotny
5. E. Ferrari
6. Thomas D. Hurley
7. E. Casali
8. J. A. Patel

Citations in the corpus

• High resolution X‐ray structures of mouse major urinary protein nasal isoform in complex with pheromones (2010, background): “tion to MUP-ligand binding even though the MUP cavity is largely hydrophobic.(20,26,27,29,31,40,41) When”
• The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes. (2009, methodology): “Table 1 summarises the dissociation constant data for the binding of these ligands to MUP available in the literature [14–19] and determined in this work.”