Lab Website: http://surmelilab.iyte.edu.tr/
Office: Science Faculty Building, Block A, Office No 205
Phone: (232) 750-7383
Nur Başak Sürmeli, PhD
Assistant Professor, Department of Bioengineering
Dr. Surmeli received her B.Sc. in Chemistry from Bilkent University in 2003. She then moved on to Princeton University to complete her Ph.D. in Chemistry in 2009. At Princeton, she worked with Prof. John T. Groves, studying the molecular mechanisms of metalloprotein interactions with reactive oxygen and nitrogen species. She then started her postdoctoral research in Prof. Michael A. Marletta’s laboratory at University of California, Berkeley. She moved with his laboratory to The Scripps Research Institute. Here, she studied the enzyme soluble guanylate cyclase (sGC), the cellular receptor for the signaling molecule nitric oxide (NO). She joined the Bioengineering Department in 2015 as an Assistant Professor.
Recent advancements in molecular biology and genetics has led to the interdisciplinary field of protein engineering. The aim of protein engineering is to use fundamental principles of engineering, techniques of molecular biology and chemistry to obtain new molecules with specific properties. Protein engineering is applied in discovery of novel drugs, production of fine chemicals, novel transgenic plants and nanotechnology. Surmeli Lab focuses of design of novel biocatalysts from metalloprotein scaffolds to use in production of pharmaceuticals and fine chemicals.
N.B. Surmeli, F.M. Muskens, M.A. Marletta,“The Influence of Nitric Oxide on Soluble Guanylate Cyclase Regulation by Nucleotides: the Role of Pseudosymmetric Site”, Journal of Biological Chemistry, 290, 25, 15570-80, 2015
N.B. Surmeli, M.A. Marletta, “Insight into the rescue of oxidized soluble guanylate cyclase by the activator cinaciguat.”, Chembiochem, 13, 7, 977-81, 2012
N.B. Surmeli, N.K. Litterman, A.F. Miller, J.T. Groves, “Peroxynitrite mediates active site nitration in manganese superoxide dismutase. Evidence for the role of carbonate radical anion”, Journal of the American Chemical Society, 132, 48, 17174-17185, 2010