Karim Fahmy (0000-0002-8752-5824)

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Our lab is interested in the physical factors that modulate the structure of soluble and membrane-inserted proteins. Using model systems of G protein-coupled receptors and ion transporters we study the role of interfacial water in regulating transmembrane helix position, intra-membrane protein hydration and orientation of amino acid side chains at the mambrane surface. Collective properties of membrane lipids such as lateral pressure and acyl chain packing are studied by a combination of fluorescence and infrared spectroscopic methods. Recently, we extended our work to metal ion-induced folding in natural proteins using circular dichroism and luminescence spectroscopy of lanthanides.

Structural and energetic aspects of the hydration shell of biomolecules, including DNA and DNA origami, are specifically addressed in experiment and theory.

Finally, we study by microcalorimetry the influence of lipids and metal ions on microbial metabolism. Novel calorimetric evaluation methods are developed in our lab to determine the energetic cost of specific metabolic pathways.

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Helmholtz-Zentrum Dresden-Rossendorf: Dresden, Sachsen, DE

2002 to present

Employment

Karim Fahmy

https://orcid.org/0000-0002-8752-5824

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Biography

Activities

Employment (2)

Helmholtz-Zentrum Dresden-Rossendorf: Dresden, Sachsen, DE

Albert-Ludwigs-Universität Freiburg: Freiburg im Breisgau, Baden-Württemberg, DE

Education and qualifications (5)

University of Freiburg: Freiburg im Breisgau, DE

The Rockefeller University: New York, NY, US

Albert-Ludwigs-Universität Freiburg: Freiburg im Breisgau, Baden-Württemberg, DE

Ruhr-Universität Bochum: Bochum, Nordrhein-Westfalen, DE

Philipps-Universität Marburg: Marburg, Hessen, DE

Professional activities (1)

Philipps University of Marburg: Marburg, DE

Funding (2)

Molekulare Mechanismen der Interaktion chaotroper Salze mit natürlichen und künstlichen DNA-Strukturen

Infrarot und fluoreszenzspektroskopische Untersuchung molekularer Erkennungsprozesse bei der Rezeptor-G-Protein-Kopplung und beim Stoff- und Ionentransport durch Biomembranen

Works (10)

Exploring Antibacterial Activity and Bacterial-Mediated Allotropic Transition of Differentially Coated Selenium Nanoparticles

Special Issue “Advances in Monitoring Metabolic Activities of Microorganisms by Calorimetry”

Distinct Effects of Chemical Toxicity and Radioactivity on Metabolic Heat of Cultured Cells Revealed by “Isotope-Editing”

Interdisciplinary biophysical studies of membrane proteins bacteriorhodopsin and rhodopsin

Anion-specific structure and stability of guanidinium-bound DNA origami

Simple Growth–Metabolism Relations Are Revealed by Conserved Patterns of Heat Flow from Cultured Microorganisms

Dipolar Relaxation Dynamics at the Active Site of an ATPase Regulated by Membrane Lateral Pressure

The Molecular Switching Mechanism at the Conserved D(E)RY Motif in Class-A GPCRs

Paramagnetic Decoration of DNA Origami Nanostructures by Eu<sup>3+</sup> Coordination

Lipid Protein Interactions Couple Protonation to Conformation in a Conserved Cytosolic Domain of G Protein-coupled Receptors

Peer review (3 reviews for 2 publications/grants)