Conformational variability of benzamidinium-based inhibitors.

ABSTRACT: Determining the structure of a small molecule bound to a biological receptor (e.g., a protein implicated in a disease state) is a necessary step in structure-based drug design. The preferred conformation of a small molecule can change when bound to a protein, and a detailed knowledge of the preferred conformation(s) of a bound ligand can help in optimizing the affinity of a molecule for its receptor. However, the quality of a protein/ligand complex determined using X-ray crystallography is dependent on the size of the protein, the crystal quality, and the realized resolution. The energy restraints used in traditional X-ray refinement procedures typically use "reduced" (i.e., neglect of electrostatics and dispersion interactions) Engh and Huber force field models that, while quite suitable

SUBMITTER: Li X 

PROVIDER: S-EPMC2730048 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature