Zaměstnanci

Jméno Heyda Jan
Pozice Ph.D. Student
Jan Heyda

Jan Heyda

Ph.D. student


Laboratory of Pavel Jungwirth
Institute of Organic Chemistry and Biochemistry ASCR, v.v.i.
Flemingovo nám. 2, CZ-166 10 Prague 6, Czech Republic

Phone: (+420) 220 410 314
Fax: (+420) 224 410 320

 
Education
since 2007 Faculty of Science, Charles University in Prague (study program Physical Chemistry; Simulation of chemical properties of nano- a biostructures).
since 2007 International Max Planck Research School for "Dynamical Processes in Atoms, Molecules and Solids" in Dresden.
2011 (3 months) Advanced level course "Statistical Mechanics with focus on Liquids, Solutions and Colloidal Systems" at the University of Gothenburg, Sweden.
2002-2008 M.Sc. in Mathematics at the Faculty of Mathematics and Physics at Charles University in Prague (study program: Mathematical Modeling in Physics and Engineering).
2002-2007 M.Sc. in Chemistry at the Faculty of Science, Charles University in Prague (study program Physical Chemistry, group Electromigration and Separation Methods).
 
Experience
2006-2008 Work in program COMSOL Multiphysics with respect to numerical solution of partial-differential equations (coupled convection-diffusion equations for weak electrolytes).
2007-2008 Fundamental Research Project with Agilent Technologies Company.
 
Appointments
since 2007 Ph.D. student, Institute of Organic Chemistry and Biochemistry v.v.i., Academy of Sciences of the Czech Republic, Prague.
 
Teaching
2007 Exercises to the course "Classical molecular dynamics" at Charles University in Prague.
2008 Lecture contribution to the course "Advanced Methods in Molecular Dynamics" at Charles University in Prague.
 
Research interest
Salt (including buffers), osmolyte, and denaturant solutions affect physical (solubility, conformational stability), but also bio-chemical (enzymatic activity) properties of peptides, proteins and enzymes. Understanding of the ion-specific effects is therefore of primary importance.
  • Molecular dynamics simulations of ions at aqueous interfaces, particularly interactions of ions and osmolytes with protein surfaces and protein-proxy species.
  • Statistical thermodynamic connection of simulation with experimentally measurable quantities.