SKRBIC Tatjana

Qualifica Assegnista
Telefono 041 234 8961
E-mail tatjana.skrbic@unive.it
Sito web www.unive.it/persone/tatjana.skrbic (scheda personale)
 https://sites.google.com/a/unive.it/home-page-of-tatjana-skrbic
Struttura Dipartimento di Scienze Molecolari e Nanosistemi
Sito web struttura: https://www.unive.it/dsmn
Research Institute Research Institute for Complexity


Tatjana Skrbic
Post-doc in computational biophysics

Department of Molecular Sciences and Nanotechnology
University of Venice
Italy

Tel: +39 041 234 8961
e-mail: tatjana.skrbic@unive.it


Personal information

Date and place of birth: 28th September 1977, Subotica, Serbia
Citizenship: Serbian, Hungarian (EU)
Residency: permanent Italian residency
Maritual status: married (maiden family name Tosic), two children


Education

International School for Advanced Studies (SISSA), Trieste, Italy
Ph.D. in Physics, (2005 - 2009)
"Dynamics of doped He-4 and He-3 clusters from reptation quantum Monte Carlo"
Supervisors: Dr. Saverio Moroni and Prof. Stefano Baroni

International School for Advanced Studies (SISSA), Trieste, Italy
M.Sc. in Physics, (2004 - 2005)
Thesis title: "Satellite bands in the roto-vibrational spectra of helium
solvated carbon-dioxide"
Supervisors: Dr. Saverio Moroni and Prof. Stefano Baroni

University of Novi Sad, Novi Sad, Serbia
B.Sc. in Physics (1996 - 2000)
Thesis title: "Low-temperature properties of super-lattice with double
Heisenberg antiferromagnetic layer"
Supervisor: Prof. Darko Kapor


Scientific Employment & Academic Responsibility

Department of Molecular Sciences and Nanotechnology, University of Venice, Venice, Italy
Postdoc in a group of Prof. Achille Giacometti
(2014 - to date)

Physics and Astronomy Department "Galileo Galilei", University of Padova, Padova & SISSA, Trieste, Italy
Postdoc, Statistical Physics Sector, Supervisors: Prof. Antonio Trovato and Prof. Alessandro Laio
(2012 - 2014)


I have participated in the project "Innovative tools for cancer risk assessment
and early diagnosis" funded by AIRC (Associazione Italiana per la Ricerca sul Cancro),
on the development of computational protocol that predicts the binding affinities of protein complexes,
starting from the structural information only.

Interdisciplinary Laboratory for Computational Science (LISC) & Department of Physics, University of Trento, Trento, Italy
Postdoc, Statistical Biophysics Sector in the group of Prof. Pietro Faccioli
(2010 - 2012)

International School for Advanced Studies (SISSA), Trieste, Italy
PhD student, Condensed Matter Sector, Head: Prof. Stefano Baroni
(2004 - 2009)

University of Novi Sad, Department of Physics, Novi Sad, Serbia
Research Assistant (2001 - 2004)

University of Novi Sad, Department of Physics, Novi Sad, Serbia
Teaching Assistant (2001 - 2002)

University of Novi Sad, Faculty of Engineering, Novi Sad, Serbia
Teaching Assistant (2002 - 2004)

Serbian Physical Society, Belgrade, Serbia
Member of Physical Contests board for secondary schools
(2001 - 2003)


Research Interests & Projects Descriptions


Predicting the binding affinities of protein complexes

Protein-protein interactions play an essential role in the biological function of many proteins.
Recently, a non-redundant set of non-obligatory protein complexes has become available for which
the binding affinities and the structures of both the protein complex and its free components are
determined [1,2]. This set is diverse in terms of both the binding affinities
that span nine orders
of magnitude and the biological functions of the reported complexes and thus represents an ideal benchmark
to test theoretical methods and predictions.

The recently reported BACH statistical potential [3], based on residue pair contact
energies and single
residue solvation energies, showed excellent performances in discriminating the native states of monomeric
proteins among large sets of alternative conformations. We employ the above set of experimental structures to
test a new flavor of the BACH potential with the aim to predict the binding affinities of protein complexes.
The latter is in general a very difficult task [1,4] and we will show how three distinct
features are needed
to improve the predictive performance of our method. The first is the introduction of a novel residue-residue
contact class that distinguishes the polar and apolar nature of interaction of contacting side chain atoms.
The second is averaging the BACH scoring function over thermal fluctuations, as estimated from molecular
dynamics (MD) simulations initiated from the experimental structures [3]. Finally, we will discuss
the crucial role of entropic corrections to the free energy of binding,
focusing in particular on the vibrational entropy
evaluated by means of coarse-grained elastic network models. A fundamental step in our method involves the
finding for each single structure, either a complex or a free subunit, of the proper elastic constant to be used
in the network model. This is achieved through the matching of the residue mobilities predicted via the
network model with the mobilities obtained via MD simulations. Overall, our results emphasize the importance
of vibrational entropy in the binding process of non-obligatory complexes.


[1] "Are scoring functions in protein-protein docking ready to predict
interactomes? Clues from a novel binding affinity benchmark", P. Kastritis and Alexandre Bonvin,
J. Proteom Res. 9, 2216 (2010).

[2] "A structure-based benchmark for proteinÐprotein binding affinity", P. Kastritis, I. Moal, H. Hwang, Z. Weng, P. Bates, A. Bonvin and J. Janin,
Protein Sci. 20, 482 (2011).

[3] "A simple and efficient statistical potential for scoring ensembles of protein structures",
P. Cossio, D. Granata, A. Laio, F. Seno and A. Trovato, Sci. Rep. 2, 351 (2012).

[4] "Protein-protein binding affinity prediction on a diverse set of structures",
I. Moal, R. Agius and P. Bates, Bioinformatics 27, 3002 (2011).


Non-equilibrium dynamics of biomolecules and protein folding

The dynamics of complex, thermally driven systems, like biomolecules or
chemical reactions, shares several important features with quantum systems, in which
the behavior is intrinsically non-deterministic. In view of these analogies, the
so-called Dominant Reaction Pathways (DRP) approach [1] was developed to study
the
low-energy dynamics of soft condensed matter systems of biological interest, namely
protein folding reaction. This approach allows one to bypass the problem of the
presence of large number of very different time-scales (that limits the practical
application of Molecular Dynamics), by adopting the path space description. The DRP
framework allows to very efficiently compute the statistically most significant
pathways that connect given denaturated configurations to the native state at an atomic
level of detail and employing realistic force fields.

The project that I was involved with is the calculation of the dominant
folding pathways of the protein consisting of three antiparallel beta-strands,
namely the Fip35 WW domain, using DRP approach with atomistically detailed force field
and coarse-grained models [2]. Our results showed that the folding trajectories
are not heterogeneous, but rather suggest that the folding
proceeds through two dominant channels, defined in a hierarchical order of hairpin
formation. This result is in agreement with the Weikl's analysis of kinetic experiments
[3], as well as with the Krivov's analysis [4] of
the ms-long equilibrium MD simulations of this system performed on a special-purpose
supercomputer [5]. Our results also suggest that the choice of the folding
pathway is strongly correlated with the structure of the denaturated configuration from
which the reaction is initiated.

[1] "Dominant Pathways in Protein Folding", P. Faccioli, M. Sega, F. Pederiva and H. Orland,
Phys. Rev. Lett. 97, 108101 (2006).

[2] "Dominant Folding Pathways of a WW Domain",  S. a Beccara, T. Skrbic, R. Covino, and P.Faccioli,
Proc. Natl. Acad. Sci. USA 109, 2330 (2012).

[3] "Transition states in protein folding kinetics: Modeling phi-values of small beta-sheet proteins",
T. R. Weikl, Biophys. J. 94, 929 (2008).


[4] "The Free Energy Landscape Analysis of Protein (FIP35) Folding Dynamics", S. V. Krivov,
J. Phys. Chem. B 115, 12315 (2011).

[5] "Atomic-Level Characterization of the Structural Dynamics of Proteins",
D. E. Shaw, P. Maragakis, K. Lindorff-Larsen, S. Piana, R. O. Dror,
M. P. Eastwood, J. A. Bank, J. M. Jumper, J. K. Salmon, Y. Shan and W. Wriggers,
Science 330, 341 (2010).


Folding of topologically self-entangled proteins

The proteins with topologically non-trivial native structure (knotted proteins),
represent an ideal playground to investigate the interplay of enthalpy and entropy during the
folding process. Thus we have been examining the folding mechanism that leads to
the formation of knots in proteins [1-3].


Firstly, we have employed the stochastic Monte Carlo
scheme within a coarse-grained model (on the amino-acid level) that  employes the
potential energy function that has both native-centric part [4] and the
non-native part [5], based on statistical potentials that measure the propensity
of a given amino-acid pair to form a contact.

We have concentrated on the early stage of the folding transition of two
homologous proteins, one of which displays the knot in its native state. We find that
the non-native interactions promote the formation of knots in the denaturated state of
the protein with a topologically non-trivial native structure, consistently with recent
experimental studies that suggest that the denaturated ensemble of the natively knotted
proteins have high propensity to be knotted [6]. On the other hand, the same interactions
have no effect in the unknotted protein. In addition, we find that if the non-native
interactions are neglected, no knot is formed in the denaturated state of either protein.
We argue that the knotting occurs through the threading of the alpha-helix near the
C-terminal through unspecific loops, formed in the inner region of the chain. The same
effects are also observed in the folding of two other knotted proteins, which have
different length and belong to different families.

Secondly, we have performed the first atomistic simulation of the folding of a knotted protein within
a realistic force field. We have found that, apart from promoting knots, non-native interactions modify
the structure of the folding pathways. This effect is quite surprising, because the inclusion of
non-native interactions is expected to increase the degree of frustration in the potential energy landscape.
One therefore expects that this would lead to a greater entropy of the ensemble of folding pathways.
The fact that they are found to suppress the folding heterogeneity may be interpreted that even non-native
interactions may act in a cooperative way [1,3].


[1] "The Role of Non-Native Interactions in the Folding of Knotted Proteins:
Insights from Molecular Dynamics Simulations", R. Covino, T. Skrbic, S. a Beccara, P. Faccioli and C. Micheletti,
Biomolecules 4, 1 (2014).

[2] "Folding Pathways of a Knotted Protein with a Realistic Atomistic Force Field",
S. a Beccara, T. Skrbic, R. Covino, C. Micheletti and P. Faccioli,
PLoS Comp. Biol. 9,  e1003002 (2013).

[3] "The Role of Non-native Interactions in the Folding of Knotted Proteins",
T. Skrbic, C. Micheletti and P. Faccioli, PLoS Comp. Biol. 8, e1002504 (2012).

[4] "The origins of the asymmetry in the folding transition states of protein l and protein G",
J. Karanicolas and C. L. Brooks, Protein Sci. 11, 2351 (2002).

[5] "Coarse-grained models for simulations of multi-protein complexes:
application to ubiquitin binding", Y. C. Kim and G. Hummer,  J. Mol. Biol. 375, 1416 (2008).

[6] "Experimental detection of knotted conformations in denaturated proteins",
A. L. Mallam, J. M. Rogers, and S. E. Jackson, Proc. Natl. Acad. Sci. USA 107, 8189 (2010).


Thermal adaptation of cystein-rich proteins

In order to survive in a permanently cold environment, psychrophilic microorganisms synthesize proteins
that are resistant to cold-induced denaturation and misfolding [1]. On the other hand, the native states of these proteins
are often only marginally stable, or even unstable in temperate environments. This case clearly illustrates how, in order to understand
at the molecular level the principles that regulate the adaptation of microorganisms to different thermal environments, it is crucial to
identify the general physical principles that shape the structure of the proteins' free-energy landscapes. From this perspective, it is
particularly useful to compare the folding thermodynamics of homologous proteins produced by species which are evolutionarily closely
related, yet ecologically separated, such as are species living, one, in polar waters and, the other one, in temperate waters. In this way,
it appears to be easier, at least in principle, to identify specific structural features that are more directly responsible for the thermodynamic
stability of the protein native state.


We have studied protein unfolding/refolding thermodynamics by means of Monte Carlo (MC) simulations in a coarse-grained native-centric
model, that complements a recent analysis of circular dichroism (CD) spectra [2] of two closely homologous families of water-borne
signaling proteins (known as pheromones), which regulate the vegetative (mitotic) growth and sexual mating [3] in two
ecologically separated {\it Euplotes} species, {\it E. raikovi} (mesophilic) living in temperate waters and {\it E. nobilii} (psychrophilic) living
in polar (Antarctic and Arctic) waters [4].

CD measurements [2] indicated that in the {\it E. nobilii} pheromones the alpha-helical content decreases drastically in the
temperature range from 55 C to 70 C . By contrast, in {\it E. raikovi} pheromones this fraction remains almost
unaltered even at 100 C. Based on the results of MC simulations we were led to the conclusion that the observed enhanced
stability of the {\it E. raikovi} pheromones is due to the non-local pattern of topological constrains determined by the disulfide bonds, which reduce
the conformational entropy gain in unfolding the secondary structures. To allow for further experimental assessment of our conclusions we designed
an {\it E. nobilii} pheromone mutant, which is expected to unfold at a very high temperature like {\it E. raikovi} pheromones.


[1] "Psychrophilic microorganisms: Challenges for life", S. D'Amico, T. Collins, J. Marx, G. Feller and C. Gerday,
Embo. Rep. 7, 385 (2006).

[2] "Thermodynamic stability of psychrophilic and mesophilic pheromones of the protozoan ciliate Euplotes",
M. Geralt, C. Alimenti, A. Vallesi, A., P. Luporini and K. Wuthrich, Biology 2, 142 (2013).

[3] "Autocrine mitogenic activity of pheromones produced by the protozoan ciliate Euplotes raikovi",
A. Vallesi, G. Giuli, R. A. Bradshaw and P. Luporini, Nature 376, 522 (1995).

[4] "Antarctic and Arctic populations of the ciliate Euplotes nobilii show common pheromone-mediated cell-cell
signaling and cross-mating", G. Di Giuseppe, F. Erra, F. Dini, C. Alimenti, A. Vallesi, B. Pedrini, K. Wuthrich and P. Luporini,
Proc. Natl. Acad. Sci. USA 108, 3181 (2011).

[5] "Unfolding Thermodynamics of Cysteine-Rich Proteins and Molecular Thermal-Adaptation of Marine Ciliates",
G. Cazzolli, T. Skrbic, G. Guella and P. Faccioli, Biomolecules 3, 967 (2013).


Quantum dynamics of helium droplets

During my PhD studies I have applied different flavours of quantum Monte
Carlo methods (variational, diffussion, path-intagral and reptation [1]
to study the dynamics of helium droplets doped with molecular impurities [2].
Namely, I was involved in the calculations of rotational excitations of
these systems. In particular, I was devising
symmetry-adapted imaginary-time correlation functions to study the rotational spectrum
of doped He-4 clusters within the frame of the reptation
quantum Monte Carlo method. The success of this approach relies on the choice of suitable
correlation functions, whose spectral resolution is dominated by few, well separated
eigenvalues of the Hamiltonian. Under these conditions, reliable excitation energies
can be extracted by inverse Laplace transform. This method has been tailored for bosons,
due to the positivity of the ground-state wave-function and to the distinctive scarcity
of low-lying states. For sufficiently small systems, however, the states of the discrete
spectrum can be calculated in the same manner also with Fermi statistics, using
appropriate generalizations of the correlation functions, so that rotational spectra of
doped He-3 clusters could be extracted.


[1] "Reptation Quantum Monte Carlo: A Method for Unbiased Ground-State
Averages and Imaginary-Time Correlations", S. Baroni and S. Moroni,
Phys. Rev. Lett. 82, 4745 (1999).

[2] "Structure, Rotational Dynamics and Superfluidity of Small
OCS-Doped He Clusters", S. Moroni, A. Sarsa, S. Fantoni, K. E. Schmidt and S. Baroni,
Phys. Rev. Lett. 90, 143401 (2003).

[3] "Unraveling Excited States of Doped Helium Clusters", T. Skrbic, S. Moroni and S. Baroni,
J. Phys. Chem. A 111, 12749 (2007).

[4] "Computational Spectroscopy of Carbon Monoxide Isotopomers in Helium Clusters",
T. Skrbic, S. Moroni and S. Baroni, J. Phys. Chem. A 111, 7640 (2007).


Workshops, Schools, Conferences & Seminars

Societa' Italiana di Fisica, Varenna, Italy
International School of Physics "Enrico Fermi", July 2015.

Max Planck Institute for Polymer Research, Mainz, Germany
Conference "Mainz Simulation Days 2015", June 2015.

Societa' Italiana di Biochimica e Biologia Molecolare, Padova, Italy
Conference "Proteine 2014", April 2014.
"Predicting the Binding Affinities of Protein Complexes: the role of vibrational entropy",
poster contribution & best poster award

3rd National Workshop, Bressanone, Italy
"Protein Physics: Structure, Dynamics and Function", February 2014.
"Predicting the Binding Affinities of Protein Complexes: the role of entropic contributions", talk contribution

Italian National Conference on Condensed Matter Physics, FisMat 2013, Milano, Italy
Politecnico di Milano, September 2013.
"Knotted Proteins: Folding Pathways and the Role of Non-native Interactions", talk contribution
and "Predictiong the Binding Affinities of Protein Complexes", poster contribution

Physics and Astronomy Department "Galileo Galilei", University od Padova, Padova, Italy
Statistical Physics Seminar, October 2012.
"Protein Folding: from Coarse-Grained to Atomistic Simulations"

XIII International Workshop on Complex Systems, Andalo, Italy
Session: Bio-systems, March 2012.
"Studying the folding of knotted proteins by Monte Carlo simulations", talk contribution

Aalto University, Department of Applied Physics, Helsinki, Finland
Multiscale Statistical Physics Group, Head: Prof. Tapio Ala-Nissila
March 2012
"Path-integral Methods: from Computational Spectroscopy to Protein Folding
Pathways", invited seminar

Workshop: Computational Science in Trento, Trento, Italy
"Advanced Comp. Methods for Materials Science and Biomolecular Systems", November 2011.
"Studying the folding of knotted proteins by Monte Carlo simulations", talk contribution

Meeting of Postdocs in Nuclear Physics and Superfluidity, Trento, Italy
Discussion Day, October 2011.
"Simulating protein folding", talk contribution

8th EBSA European Biophysics Congress, Budapest, Hungary
Session: "Computational Biophysics and Simulation", August 2011.
"The role of non-native interactions in knotted proteins", talk contribution

SISSA Workshop, Trieste, Italy
"Structural Bioinformatics and Computational Biophisics", July 2011.

ECT* International Workshop, Trento, Italy
"Applications of Theoretical Physics Methods in Biology", June 2010.
"Coarse-grained models for dynamics and thermodynamics of protein-protein and
protein-membrane interactions", talk contribution

1st National Workshop, Bressanone, Italy
"Physics of Protein Folding and Aggregation", February 2010.

2nd Mini Workshop, Sardagna, Italy
"Quantum Monte Carlo Methods", December 2008.
"Rotational spectrum of small doped He-3 clusters",
poster contribution

APS March Meeting, New Orleans, USA
Focus Session: "Photophysics of Cold Molecules III", March 2008.
"Rotational spectrum of small doped He-3 clusters", talk contribution

Joint ICTP/Democritos Winter School, Trieste, Italy
"Advanced School on Quantum Monte Carlo Methods in Physics and Chemistry", January 2008.
"Unraveling excited states of doped helium clusters", poster contribution

1st Mini Workshop, Sardagna, Italy
"Quantum Monte Carlo Methods", December 2006.
"Satellite bands in the roto-vibrational spectra of molecules in helium
nanodroplets", poster contribution

Joint ICTP/Democritos Winter School, Trieste, Italy
"Continuum Quantum Monte Carlo Methods", January 2004.

5th General Conference of the Balcan Physical Union (BPU-5), Vrnjacka Banja, Serbia
Serbian Physical Society, August 2003.
"Density relaxation in a vibrated granular material: numerical simulation", poster contribution
"Monte Carlo study of magnetic and thermal properties of thin ferromagnetic films with uniaxial anisotropy", poster contribution

National Symposium of Condensed Matter Physics, Arandjelovac, Serbia
Serbian Physical Society, October 2001.
"The dependence of the critical temperature T_C, T_N on the width (number of layers) of ferro- and
antiferromagnetic films", poster contribution
"Analysis of 3d-2d crossover in layered antiferromagnets depending on
spin and spatial anisotropy", poster contribution


Publications

Peer Reviewed Articles

"From Polymers to Proteins: the effect of side-chains and cylindrical symmetry on the formation of
secondary structures within a Wang-Landau approach", Tatjana Skrbic, Artem Badasyan, Trinh Xuan Hoang,
Rudolf Podgornik and Achille Giacometti, submitted to Soft Matter


"Predicting the Binding Affinities of Protein Complexes: the role of vibrational entropy",
Tatjana Skrbic, Edoardo Sarti, Stefano Zamuner, Flavio Seno, Alessandro Laio and Antonio Trovato,
submitted to PLoS ONE

"The Role of Non-Native Interactions in the Folding of Knotted Proteins:
Insights from Molecular Dynamics Simulations",
Silvio a Beccara,  tatjana Skrbic, Roberto Covino, Cristian Micheletti and Pietro Faccioli,
Biomolecules 4, 1 (2014).

"Unfolding Thermodynamics of Cysteine-Rich Proteins and Molecular Thermal-Adaptation of Marine Ciliates",
Giorgia Cazzolli, Tatjana Skrbic, Graziano Guella and Pietro Faccioli,
Biomolecules 3, 967 (2013).

"Folding Pathways of a Knotted Protein with a Realistic Atomistic Force Field",
Silvio a Beccara, Tatjana Skrbic, Roberto Covino, Cristian Micheletti and Pietro Faccioli,
PLoS Comp. Biol. 9, e1003002 (2013).

"The Role of Non-native Interactions in the Folding of Knotted Proteins", Tatjana Skrbic, C. Micheletti and P. Faccioli,
PLoS Comp. Biol. 8, e1002504 (2012).

"Dominant Folding Pathways of a WW Domain", Silvio a Beccara, Tatjana Skrbic, Roberto Covino and Pietro Faccioli,
Proc. Natl. Acad. Sci. USA 109, 2330 (2012).

"Unraveling Excited States of Doped Helium Clusters", Tatjana Skrbic, Saverio Moroni and Stefano Baroni,
J. Phys. Chem. A 111, 12749 (2007).

"Computational Spectroscopy of Carbon Monoxide Isotopomers in Helium Clusters", Tatjana Skrbic, Saverio Moroni and Stefano Baroni,
J. Phys. Chem. A 111, 7640 (2007).

"Adsorption, desorption and diffusion of extended objects on a square lattice", Ljuba Budinski-Petkovic and Tatjana Tosic,
Physica A 329, 350 (2003).

"Compensation Temperatures in Systems with Three and Four Sublattices and Superlattices", Milica Pavkov, Milan Pantic, Marijana Kircan and Tatjana Tosic, J. Res. Phys. 29, 67 (2002).

"Parametrization of Albedo over Heterogeneous Surfaces in Coupled Land-Atmosphere Schemes for Environmental Modelling",
Dragutin Mihailovic, Darko Kapor, Christian Hogrefe, Jelena Lazic and Tatjana Tosic, Env. Fluid Mech. 4, 57 (2004).


Conference proceedings

"Knotted Proteins: Folding Pathways and the Role of Non-native Interactions",
Tatjana  Skrbic, Book of Abstracts: Italian National Conference on Condensed Matter Physics
FisMat 2013, 9-13 September 2013, Milano, Italy

"Studying the folding of knotted proteins by Monte Carlo simulations",
Tatjana Skrbic, Book of Abstracts: XIII International Workshop on Complex Systems,
18-22 March 2012, Andalo, Italy

"The role of non-native interactions in the folding of knotted proteins",
Tatjana Skrbic, Cristian Micheletti and Pietro Faccioli,
Proceedings of the 8th EBSA European Biophysics Congress,
Eur. Biophys. J. 40, Suppl. 1 (2011) 3, DOI: 10.1007/s00249-011-0730-3

"Satellite bands in the rotational spectrum of doped helium clusters",
Tatjana Skrbic, Saverio Moroni and Stefano Baroni,
Bulletin of the American Physical Society on the occasion
of the 2006 APS March Meeting, http://meetings.aps.org/link/BAPS.2006.MAR.Q1.238

"Rotational spectrum of small, doped He-3 clusters",
Tatjana Skrbic, Saverio Moroni and Stefano Baroni,
Bulletin of the American Physical Society on the occasion of the
2008 APS March Meeting, http://meetings.aps.org/link/BAPS.2008.MAR.D26.4

"Density relaxation in a vibrated granular material--numerical simulation",
Ljuba Budinski-Petkovic and tatjana Tosic,
Proceedings of BPU-5, the Fifth General Conference of the Balcan Physical Union,
25-29 August 2003, Vrnjacka Banja, Serbia

 "Monte Carlo study of magnetic and thermal properties of thin ferromagnetic
films with uniaxial anisotropy",
Ljuba Budinski-Petkovic and Tatjana Tosic,
Proceedings of BPU-5, the Fifth General Conference of the Balcan Physical Union,
25-29 August 2003, Vrnjacka Banja, Serbia

"Analysis of 3D-2D Crossover in Layered Antiferromagnets Depending on Spin
nd Spatial Anisotropy", Milica Pavkov, Tatjana Tosci, Marijana Kircan, Darko Kapor and Mario Skrinjar,
Proceedings of SFKM, Symposium of Condensed Matter Physics, 3-5 October 2001, Arandjelovac, Serbia

"The Dependence of the Critical Temperature T_, T_N on
the Width (number of layers) of Ferro- and and Antiferromagnetic Films",
Tatjana tosic, Darko Kapor and Mario Skrinjar,
Proceedings of SFKM, Symposium of Condensed Matter Physics, 3-5 October 2001,
Arandjelovac, Serbia

"An Approach for the Aggregation of Albedo in Calculating
the Radiative Fluxes over Heterogeneous Surfaces in Atmospheric Models",
Proceedings of the Integrated Assessment and Decision Support (iEMSs) Conference,
session on the "Environmental modelling of physical, biophysical and chemical
processes as a component of soil-plant", 24-27 June 2002, Lugano, Switzerland