A study from the Michael Chapman lab titled “Parsimony in protein conformational change,” published in the journal Structure, provides a more complete picture of how proteins move. The researchers used nuclear magnetic resonance spectroscopy to better understand the dynamics of protein movement and thus get a better view of their normal functioning. The team designed a computer method that looks at two different snapshots of the same protein structures. Some of the findings: Minimal torsion angle rotations are a major characteristic of conformational change–and large changes are composed of smaller dihedral rotations.
The senior author, Michael Chapman, Ph.D., is professor of biochemistry and molecular biology, in the OHSU School of Medicine and a member of the OHSU Knight Cancer Institute. The study bridges a significant gap in knowledge that will help determine what – at the molecular level – causes disease and how best to treat those illnesses. The long-term results of this work may provide a foundation for the development of more effective drug treatments.
Read the OHSU media release here.