José Faraldo-Gómez, Ph.D.
Theoretical Molecular Biophysics Section
Building 50, Room 2152
50 South Drive
Bethesda, MD 20814
The Theoretical Molecular Biophysics Section aims to help elucidate the structural mechanisms of biomedically important molecular systems associated with cellular membranes. Dr. Faraldo-Gómez and his co-workers are particularly interested in systems involved in transmembrane signaling and transport, as well as bioenergeticsenergy conversion. Either individually or in complex with others, membrane proteins mediate numerous essential processes in living cells, such as the communication between and within cells and the import and metabolism of nutrients. Consequently, a wide range of health disorders in humans, from heart disease to neurodegeneration, are associated with the malfunction of membrane-associated systems. Membrane transport proteins are also crucial for the survival of multi-drug resistant pathogenic bacteria and cancer cells, and are therefore promising pharmaceutical targets. The premise of this the research program of the Theoretical Molecular Biophysics Section is thus that a more profound detailed understanding of the molecular mechanisms of these important systems will eventually facilitate the development of effective pharmacological approaches.
The investigations carried out in theby Dr. Faraldo-Gómez group and his group rely primarily on computationally-intensive, physics-based molecular simulations as well as other theoretical methods. This work is often carried out in synergy with experimental collaborators, particularly in the areas of structural biology, biochemistry, and molecular biophysics. The goal of this multi-disciplinary approach is to characterize the structural dynamics and energetics of the molecular systems studied at atomic resolution. These insights enable the group to formulate novel mechanistic hypotheses that may be tested experimentally, or to provide realistic interpretations of existing experimental data.
On the methodological front, the group is actively involved in the development and implementation of novel approaches to extract reliable thermodynamic and mechanistic information from molecular simulations.
José Faraldo-Gómez earned a B.Sc. in Physics from the Universidad Autónoma in Madrid in 1999, and a Ph.D. in Biophysics from the University of Oxford in 2002, under the supervision of Prof. Mark Sansom. Subsequently he was a postdoctoral fellow with Prof. Benoit Roux, first at Cornell Medical College in New York and later at the University of Chicago. In late 2007 Dr. Faraldo-Gómez established the Theoretical Molecular Biophysics Group at the Max Planck Institute of Biophysics in Frankfurt, Germany, and from 2008 where he was also an Adjunct Investigator of the German Research Foundation Cluster of Excellence in Frankfurt. In 2013 he joined the NHLBI as a tenure-track investigator, where he currently leads the Theoretical Molecular Biophysics Section. Dr. Faraldo-Gómez is an Associate Editor or the Journal of General Physiology and a member of the Editorial Board of Biophysical Journal, and frequently serves as a reviewer for leading scientific journals covering the field of structural and molecular biophysics.
Ficici E, Zhou W, Castellano S, Faraldo-Gómez JD. Broadly conserved Na<sup>+</sup>-binding site in the N-lobe of prokaryotic multidrug MATE transporters. Proc Natl Acad Sci U S A. 2018;115(27):E6172-E6181.
Anselmi C, Davies KM, Faraldo-Gómez JD. --Mitochondrial ATP synthase dimers spontaneously associate due to a long-range membrane-induced force. J Gen Physiol. 2018;150(5):763-770.
Shlosman I, Marinelli F, Faraldo-Gómez JD, Mindell JA. The prokaryotic Na<sup>+</sup>/Ca<sup>2+</sup> exchanger NCX_Mj transports Na<sup>+</sup> and Ca<sup>2+</sup> in a 3:1 stoichiometry. J Gen Physiol. 2018;150(1):51-65.
Liao J, Marinelli F, Lee C, Huang Y, Faraldo-Gómez JD, Jiang Y. Mechanism of extracellular ion exchange and binding-site occlusion in a sodium/calcium exchanger. Nat Struct Mol Biol. 2016;23(6):590-599.
Leone V, Pogoryelov D, Meier T, Faraldo-Gómez JD. On the principle of ion selectivity in Na+/H+-coupled membrane proteins: experimental and theoretical studies of an ATP synthase rotor. Proc Natl Acad Sci U S A. 2015;112(10):E1057-66.
Related Scientific Focus Areas
Molecular Biology and Biochemistry
This page was last updated on September 19th, 2018