Thermodynamic analysis of binding between mouse major urinary protein-I and the pheromone 2-sec-butyl-4,5-dihydrothiazole.

By Scott D. Sharrow, M. Novotny, M. Stone. 2003

59 citations recorded by the source corpus.

Subfields: Molecular Biology, 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. Q. Zou
3. M. Novotny
4. K. Edmonds
5. Scott D. Sharrow
6. Thomas D. Hurley
7. M. A. Goodman
8. M. Stone

Citations in the corpus

• Thermodynamic consequences of disrupting a water‐mediated hydrogen bond network in a protein:pheromone complex (2005, background): “Although a large proportion of the buried intermolecular surface is hydrophobic, the binding of either MUP-I or MUP-IV to either SBT or HMH is characterized by a large favorable change in enthalpy ( H −6 to −20 kcal/mol) and a smaller unfavorable change in entropy (−T S is in the range +3 to +8 kcal”
• 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”