Institute for Integrative Genome Biology


Dimitrios MorikisDimitrios Morikis

Professor of Bioengineering

Mailing Address:

Bourns Hall /A229
University of California
Riverside, CA 92521

Phone: (951) 827-2696
Fax: (951) 827-5696
Email: dmorikis@engr.ucr.edu



B.S. Aristotle University of Thessaloniki, Greece
M.S. Northeastern University, Boston
Ph.D. Northeastern University, Boston

College/Division Affiliation:

Bourns College of Engineering

Center/Inst Affiliation(s):

Center for Plant Cell Biology
Center for Research in Intelligent Systems (CRIS)

Areas Of Expertise:

Computational Molecular Biology; Biomolecular Structure, Dynamics, Electrostatics, and Interactions; Immunophysics; Rational Peptide, Protein, and Drug Design; Structural Bioinformatics ; NMR Spectroscopy

Awards / Honors:

2011 Distinguished Educator Award, Orange County Engineering Council's (OCEC) National Engineer's week, 2/21/2011
2008  Fellow, AIMBE (American Institute for Medical and Biological Engineering)
2006  Fellow, AAAS (American Association for the Advancement of Science)
2009-04  Non-Senate Distinguished Reseacher Award, University of California, Riverside
1999-2001  NIH (National Institutes of Health) National Research Service Award-Senior Fellowship, Department of Chemistry and Biochemistry, University of California, San Diego
1993  The Scripps Society of Fellows Travel Award for best presentation at the Scripps Society of Fellows Annual Research Symposium

Research Summary:

We follow a cross-disciplinary theoretical and experimental approach, involving biophysics, structural biology, computational chemistry, structural bioinformatics, and bioengineering. Our goals are: (i) to determine structure-dynamics-interactions-function relations for peptides, proteins, protein fragments, and protein complexes, which address basic biological processes; (ii) to design peptides and small proteins with tailored properties and to determine their structure; (iii) to perform rational design for potential therapeutic agents, and (iv) to design de novo peptides of specific structural propensities. Our work is based on the exploration of the dynamic and electrostatic properties of biomolecules and biomolecular complexes using computational methods. We also use nuclear magnetic resonance methods for peptide and protein structure determination. Proteins are dynamic systems, which interact with their surrounding environment. Proteins participate in a wide range of motions and their dynamics are essential for function. Proteins interact with solvent molecules, other proteins, nucleic acids, ligands, prosthetic groups, carbohydrates, lipids, metals, ions, and small molecules. We use molecular dynamics simulations based on the solution of Newton ’s equation of motion to explore the dynamic properties of peptides, proteins, and protein complexes, such as flexibility, mobility, correlated motions, conformational transitions, and folding. Electrostatics plays a significant role in secondary, tertiary, and quaternary structure formation and stability. Electrostatics also plays a significant role in recognition and binding for the formation of protein complexes and multi-component assemblies. We use computational methods based on the solution of the Poisson-Boltzmann equation to explore the electrostatic properties of peptides, proteins, and protein complexes, such as ionization states, desolvation, Coulombic interactions, proton sharing and transfer, conformational transitions, stability, and association. Knowledge of biomolecular structure is the starting point for computational studies at atomic resolution, involving dynamics, electrostatics, thermodynamics, kinetics, and association, which in turn are essential for basic understanding of the physicochemical properties of underlying function. Structure is also the basis of our design efforts for peptides, proteins, and potential therapeutics. We use high-resolution NMR spectroscopy and restrained molecular dynamics-based simulated annealing methods to determine the structure of peptides and small proteins. We also use structural homology methods to model protein structures based on previously solved homologous structures and deposited at the Protein Data Bank. The aim of our structural bioinformatics efforts is to classify proteins according to the spatial distribution of their electrostatic properties, using a combination of structural homology, electrostatic calculations, and similarity indices.

Related Press Releases:

Selected Publications:

List of publications from PubMed and List of Publications from Personal Website


More Information

General Campus Information

University of California, Riverside
900 University Ave.
Riverside, CA 92521
Tel: (951) 827-1012

Career OpportunitiesUCR Libraries
Campus StatusDirections to UCR

Genomics Information

Institute of Integrative Genome Biology
2150 Batchelor Hall

Tel: (951) 827-7177
E-mail: Aurelia Espinoza, Managing Director