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BP: Fachverband Biologische Physik
BP 17: Posters: Protein structure and dynamics
BP 17.16: Poster
Monday, March 16, 2015, 17:30–19:30, Poster A
Protein Folding: Driving forces and external influences — •Bernhard Reuter, Pedro A. Ojeda May, and Martin E. Garcia — University of Kassel, Theoretical Physics II, Heinrich-Plett-Str. 40, 34132 Kassel, Germany
One of the most important questions of nature sciences is why a given amino acid sequence under physiological conditions mostly exists in a certain functional spatial structure - the native state. If certain proteins misfold in bigger amounts it results in serious health impairments like neurodegenerative diseases (i.e. Alzheimer's and prion diseases). In this context the question of the effect of external influences on the stability of the native state arises. To address this problem the effect of an external electric field on the peptide V3-loop 1NJ0 was analyzed by Monte Carlo simulations. It was revealed that a strong electric field induced a transition from a beta-sheet into a helix conformation. Also the effect of an spatial temperature gradient on a proteinlike designed heteropolymer was simulated using the Langevin Dynamics method showing that a temperature gradient can facilitate protein folding.