Lucy Forrest - Prototype 01

Forrest Lab

National Institute of Neurological Disorders & Stroke

Forrest Lab Website

The Forrest lab, led by NIH Investigator Dr. Lucy R. Forrest, uses computational approaches to study proteins that exist in cell membranes. We are particularly interested in understanding the function of coupled transporter proteins through an understanding of their structure. We also develop methods to better enable the prediction of functionally important properties of such proteins. See our "Software & Data" link for more details.

The group was set up in the Max Planck Institute for Biophysics in Frankfurt, Germany, in 2007, and moved to the National Institute of Neurological Disorders and Stroke (NINDS) at the National Institutes of Health (NIH) in Bethesda, MD, USA in 2013. Currently the lab comprises 4 postdocs, and a post-baccalaureate fellow. Follow our "Lab Members" link for more details.

Useful Links:

  • Forrest group profile at NINDS - with information about Research Interests
  • The Faraldo Lab ( - Our colleagues in the Theoretical Molecular Biophysics Section of NHLBI.

Lab News

Lucy honored to present the NIH Directors Seminar

Her talk on April 5th titled "Satisfying symmetry: uncovering functional insights from patterns in membrane protein structures" can be viewed here.

Simulations help characterize transporter conformations

Paper out now in J. Gen. Physiol! We used simulations with EBmetaD to rank transporter conformations according to their agreement with DEER distance distributions. In collaboration with the Ziegler and Prisner labs, with thanks the Faraldo-Gómez lab!

EncoMPASS is in the Nucleic Acids Research database issue

Read about our new database, EncoMPASS, an easy new interface and resource to analyze symmetries and relationships between membrane protein structures! 

New insights into coupling during symport

A recent collaboration with Gary Rudnick has just been accepted for publication in PNAS. We identify a key molecular interaction responsible for responding to bound ligands and required for the major transport-related conformational change. 


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