Catching a protein intermediate

摘要

A protein's function depends on structural dynamics and on the nature of the conformation intermediates that the molecule can adopt. These transient conformations can be elusive and are therefore hard to characterize. Guillaume Bouvignies et al. use a combination of relaxation dispersion nuclear magnetic resonance and Rosetta computational structure predictions to design T4 lysozyme mutations that stabilize the excited' states that are usually too transient to be observed.