Molecular dynamics study of major urinary protein–pheromone interactions: A structural model for ligand‐induced flexibility increase

By P. Macek, P. Novák, H. Křížová, L. Žídek, V. Sklenar. 2006

12 citations recorded by the source corpus.

Subfields: Atomic and Molecular Physics, and Optics, Molecular Biology, Spectroscopy

How researchers see this paper

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

1. Jane Hurst
2. M. Phelan
3. R. Beynon
4. T. Pertinhez
5. L. McLean
6. S. Armstrong
7. E. Ferrari
8. E. Casali

Citations in the corpus

• The Structure, Stability and Pheromone Binding of the Male Mouse Protein Sex Pheromone Darcin (2014, result): “The favourable enthalpy results from the binding of the SBT in the cavity rather than to a greater loss of degrees of freedom in protein upon binding; this is supported by evidence from structural studies for other MUPs where there appears to be only minimal changes in protein conformation upon pher”
• The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes. (2009, background): “MD simulations of MUP with and without the ligand SBT bound seem to suggest that changes in hydrogen bond populations, particularly involving residues in loop regions, may be responsible for dynamical changes on ligand binding in regions more distant to the binding site [24,25].”