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José D. Faraldo-Gómez, Ph.D.

Theoretical Molecular Biophysics Section

José D. Faraldo-Gómez, Ph.D.
Investigator
Theoretical Molecular Biophysics Section


Building 5635FL Room T806
5635 Fishers Ln
Rockville, MD 20852
P: +1 301 496 4854 (Rockville)/+1 301 827 4555 (Bethesda)
jose.faraldo@nih.gov

Background

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 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 Germany, and from 2008 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 a member of the editorial board of Biophysical Journal and frequently serves as a reviewer for leading scientific journals covering the field of molecular biophysics.

Research Interests

The Theoretical Molecular Biophysics Section aims to help elucidate the structural mechanisms of biomedically important molecular systems associated with cellular membranes. Dr. Faraldo-Gómez’s group is particularly interested in systems involved in transmembrane signaling and transport as well as energy 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 research is that a more profound understanding of the molecular mechanisms of these important systems will eventually facilitate the development of effective pharmacological approaches.

The investigations carried out in the Faraldo-Gómez 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.

Please click on www.faraldolab.org for more information.

Selected Publications

Two-state dynamics of the SH3-SH2 tandem of Abl kinase and the allosteric role of the N-cap.
Corbi-Verge C, Marinelli F, Zafra-Ruano A, Ruiz-Sanz J, Luque I, Faraldo-Gómez JD.
Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):E3372-80.
[Text Abstract on PubMed]

A new type of na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motif.
Schulz S, Iglesias-Cans M, Krah A, Yildiz O, Leone V, Matthies D, Cook GM, Faraldo-Gómez JD, Meier T.
PLoS Biol. 2013 Jun;11(6):e1001596.
[Text Abstract on PubMed]

Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation.
Symersky J, Pagadala V, Osowski D, Krah A, Meier T, Faraldo-Gómez JD, Mueller DM.
Nat Struct Mol Biol. 2012 May;19(5):485-91, S1.
[Text Abstract on PubMed]

Promiscuous archaeal ATP synthase concurrently coupled to Na+ and H+ translocation.
Schlegel K, Leone V, Faraldo-Gómez JD, Müller V.
Proc Natl Acad Sci U S A. 2012 Jan 17;109(3):947-52.
[Text Abstract on PubMed]

Evidence for an allosteric mechanism of substrate release from membrane-transporter accessory binding proteins.
Marinelli F, Kuhlmann SI, Grell E, Kunte HJ, Ziegler C, Faraldo-Gómez JD.
Proc Natl Acad Sci U S A. 2011 Dec 6;108(49):E1285-92.
[Text Abstract on PubMed]

José D. Faraldo-Gómez's Full List of Publications

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Last Updated: July 16, 2014

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