Protein conformer selection by ligand binding observed with crystallography

Protein conformer selection by ligand binding observed with crystallography.

A large-scale movement between "closed" and "open" conformations of a protein loop was observed directly with protein crystallography by trapping individual conformers through binding of an exogenous ligand and characterization with solution kinetics. The buried indole ring of Trp191 in cytochrome c peroxidase (CCP) was displaced by exogenous ligands, causing a conformational change of loop Pro...

Crystallography-independent determination of ligand binding modes.

Protein-ligand interaction probed by time-resolved crystallography.

Time-resolved (TR) crystallography is a unique method for determining the structures of intermediates in biomolecular reactions. The technique reached its mature stage with the development of the powerful third-generation synchrotron X-ray sources, and the advances in data processing and analysis of time-resolved Laue crystallographic data. A time resolution of 100 ps has been achieved and rela...

Ligand complex structures in protein crystallography

Characterizing Protein/ligand Binding by DsC

All proteins are capable of recognizing and binding specific molecules such as other proteins, cofactors, prosthetic groups or drugs. Efforts to understand the mechanisms controlling selective binding were initially prompted by the realization that recognition and binding are universal features of all biochemical processes. These efforts have intensified with the awareness that knowledge-based ...