Contact Details

Forschungszentrum Jülich
ICS-6: Structural Biochemistry
52425 Jülich
Telefon: +49-2461-61-9477

Curriculum Vitae

since August 2012
Postdoc in the Computational Biochemistry Group at the ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Germany.

Postdoc in the group of Dr. Brigita Urbanc, Physics Department, Drexel University, Philadelphia, PA, USA.

Ph.D. in Physics with Dr. Ioan Kosztin, Physics and Astronomy Department, University of Missouri, Columbia, MO, USA.

Research assistant at the National Institute for Research and Development of Isotopic and Molecular Technologies, Cluj-Napoca, Romania.

M.Sc. in Applied Mathematics, Babeș-Bolyai University, Cluj-Napoca, Romania.

B.Sc. in Physics, Babeș-Bolyai University, Cluj-Napoca, Romania.

Research Interests

  • Protein aggregation in amyloid diseases
  • Protein - membrane interaction
  • Coarse-grained cell, protein and lipid modeling
  • Discrete Molecular Dynamics
  • Equilubrium and Non-equilibrium Molecular Dynamics


Fully Atomistic Aβ40 and Aβ42 Oligomers in Water: Observation of Porelike Conformatio
M.J. Voelker, B. Barz, & B. Urbanc
J. Chem. Theory Comput., DOI: 10.1021/acs.jctc.7b00495 (2017) [link]

Aβ42 pentamers/hexamers are the smallest detectable oligomers in solution
M. Wolff, B. Zhang-Haagen, C. Decker, B. Barz, M. Schneider, R. Biehl, A. Radulescu, B. Strodel, D. Willbold, & L. Nagel-Steger
Sci. Rep., 7: 2493 (2017) [link]

Conformational Transitions of the Amyloid-β Peptide Upon Copper(II) Binding and pH Changes.
Q. Liao, M. C. Owen, O. O. Olubiyi, B. Barz, & B. Strodel
Israel J. Chem., 57: 771-784 (2017) [link]

Understanding Amyloid-β Oligomerization at the Molecular Level: the Role of the Fibril Surface.
B. Barz and B. Strodel
Chem Eur J, 22, 8768-8772 (2016) [link]

Selective refinement and selection of near-native models in protein structure prediction.
J. Zhang, B. Barz, J. Zhang, D. Xu, and I. Kosztin
Proteins, 83, 1823–1835 (2015) [pdf]

Minimal model of self-assembly: emergence of diversity and complexity.
B. Barz and B. Urbanc.
J. Phys. Chem. B, 118, 3761-3770 (2014) [pdf]

Early amyloid β-protein aggregation precedes conformational change
B. Barz, O. Olubiyi, and B. Strodel.
Chem. Commun., 50, 5373-5375 (2014) [pdf]

A Kinetic Approach to the Sequence–Aggregation Relationship in Disease-related Protein Assembly
B. Barz, D.J. Wales, and B. Strodel.
J. Phys. Chem. B., 118, 1003-1011 (2014) [pdf]

Folding of Pig Gastric Mucin Non-glycosylated Domains: A Discrete Molecular Dynamics Study.
B. Barz, B. S. Turner, R. Bansil, and B. Urbanc.
J Biol Phys, 38, 681-703 (2012) [pdf]

Dimer Formation Enhances Structural Differences between Amyloid β-Protein (1–40) and (1–42): An Explicit-Solvent Molecular Dynamics Study.
B. Barz and B. Urbanc.
PLoS ONE, 7 e34345 (2012). (pdf)

Kinetic Monte Carlo and Cellular Particle Dynamics Simulations of Multicellular Systems.
E. Flenner, L. Janosi, B. Barz, A. Neagu, G. Forgacs, and I. Kosztin.
Physical Review E, 85 031907 (2012). [pdf]

Computational modeling of epithelial–mesenchymal transformations.
A. Neagu, V. Mironov, I. Kosztin, B. Barz, M. Neagu, R.A. Moreno-Rodriguez, R.R. Markwald, and G. Forgacs.
Biosystems, 100 23 (2010). [pdf]

MUFOLD: A new solution for protein 3D structure prediction.
J. Zhang, Q. Wang, B. Barz, Z. He, I. Kosztin, Y. Shang, D. Xu.
Proteins: Structure, Function, and Bioinformatics, 78 1137 (2010). [pdf]

Membrane curvature and surface area per lipid affect the conformation and oligomeric state of HIV-1 fusion peptide: A combined FTIR and MD simulation study.
B. Barz, T.C. Wong, and I. Kosztin.
Biochimica et Biophysica Acta - Biomembranes, 1778 945 (2008). [pdf]

Computational modeling of tissue self-assembly.
A. Neagu, I. Kosztin, K. Jakab, B. Barz, M. Neagu, R. Jamison, and G. Forgacs.
Modern Physics Letters B, 20 1217 (2006). [pdf]

Calculating potentials of mean force and diffusion coefficients from nonequilibrium processes without Jarzynski's equality.
I. Kosztin, B. Barz, and L. Janosi.
Journal of Chemical Physics, 124 064106 (2006). [pdf]

Local, global and electronic structure of supported gold nanoclusters determined by EXAFS, XRD and XPS methods.
N. Aldea, V. Rednic, S. Pintea, P. Marginean, B. Barz, A. Gluhoi, B.E. Nieuwenhuys, M. Neuman, X. Yaning, and F. Matei.
Superlattices and Microstructures, 46 141 (2009). [pdf]

Theoretical approach regarding nanometrology of the metal nanoclusters used in heterogeneous catalysis by powder x-ray diffraction method.
N. Aldea, B. Barz, S. Pintea, and F. Matei.
Journal Of Optoelectronics And Advanced Materials, 9 3293 (2007).

Crystalline and electronic structure of gold nanoclusters determined by EXAFS, XRD and XPS methods.
N. Aldea, P. Marginean, V. Rednic, S. Pintea, B. Barz, A. Gluhoi, B.E. Nieuwenhuys, X. Yaning, F. Matei and M. Neuman.
Journal Of Optoelectronics And Advanced Materials, 9 1555 (2007). [pdf]

Weaknesses of the pseudo-Voigt distribution used in the characterization of nanostructured materials based on the powder X-ray diffraction method.
N. Aldea, B. Barz, and F. Aldea.
Journal Of Optoelectronics And Advanced Materials, 9 651 (2007).

A new X-ray line profile approximation used for the evaluation of the global nanostructure of nickel clusters.
N. Aldea, C.V. Tiusan, and B. Barz.
Journal of Optoelectronics and Advanced Materials, 6 225 (2004).

The analysis of the interaction metal-support in Ni catalysts by extended X-ray absorption fine structure and X-ray diffraction using synchrotron radiation.
Aldea N., Barz B., Gluhoi A. C., Marginean P., Yaning X., Tiandou H., Tao L., and Wu Z.
Journal of Optoelectronics and Advanced Materials, 6 1287 (2004).

Structural and magnetic properties of polypyrrole nanocomposites.
R. Turcu, I. Peter, O. Pana, L. Giurgiu, N. Aldea, B. Barz, M.N. Grecu, and A. Coldea.
Molecular Crystals and Liquid Crystals, 417 719 (2004). [pdf]