You are here: Biocev / Research Program / Structural Biology and Protein Engineering

Structural Biology and Protein Engineering

Research Focus

1fg9_2

This program is focused on research of novel biotechnologically, diagnostically, and medically important biomolecules, proteins and nucleic acids that are constructed using state-of-the-art methods of molecular biology and protein engineering. Structures and properties of the studied molecules are analyzed by complex biophysical methods, such as advanced mass spectrometry and crystallography. Understanding structures of the studied molecules and their mutual interactions helps us to modify them to increase their desired biological activities so that they can be used for diagnostics of diseases, as drugs or as advanced materials.

 

 

Institutional research program guarantor:

Goals

1fg9_8

 

  • Newly determined 3D structures of biologically important proteins, characterization of their biophysical properties and description of their structure-activity relationships
  • Design and preparation of novel proteins developed to specifically bind to biotechnologically, diagnostically, and/or medically important molecules
  • Modifications of the studied enzymes leading to their improved function, e.g. increased temperature stability or enzymatic efficiency
  • Development of novel mass spectrometry methods, application of these methods to determination of structural and topological properties of biomolecular systems
  • Explanation of the specificity of protein/DNA interactions at atomic and submolecular scale and modifications of protein and/or DNA molecules influencing specificity of their interaction
  • Bioinformatic tools and expertise to analyse sequential and structural features of the studied biomolecules

Application potential

The program opens wide possibilities for commercial outputs. For instance, newly developed recombinant proteins with high binding affinity to other biomolecules can function as novel drugs against autoimmune diseases, viral infections or cancer or they can serve as agents to diagnose these diseases. Natural compounds will be modified with the goal to improve their antibiotic activity. Structural studies of enzymes will help increase efficiency of waste water treatment, support development of materials for green energy as biological cells, or of biotechnological treatment of food. A part of the program focused on the development of robust and sensitive methods for mass spectrometric characterization of structural and topological properties of proteins will enable fast characterization and validation of generic biologics and biosimilars.

Head of Program

Dr. Bohdan Schneider

05_Bohdan Schneider_02
  • Dr. Bohdan Schneider

  • Head of Structural Biology and Protein Engineering Program
  • Head of the Intermolecular Recognition of Proteins and Nucleic Acids Group
  • +420 325 873 766
  • curriculum vitae

Profile

Bohdan Schneider works at the Institute of Biotechnology CAS, where he focuses on protein engineering and on the study of the structure and dynamics of nucleic acids. Analysis of the structural variability of the backbone of both types of nucleic acids, DNA and RNA, has led to the determination of the local structural families of these molecules. In collaboration with colleagues he uses the knowledge of the structural behavior of nucleic acids to develop new computational methods for interpreting data from crystallographic, NMR and other biophysical measurements. He actively participated in the development of basic structural databases of biomolecules – Protein Databank and Nucleic Acid Database.

Further information can be found at http://www.structbio.org/bs

Most Significant Recent Publications

Biedermannova, L., Schneider, B. Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures. Acta Crystallographica D (2015) 71:2192-202. doi: 10.1107/S1399004715015679. ISSN 1399-0047.

Cerny, J., Biedermannova, L., Mikulecky, P., Zahradnik, J., Charnavets, T., Sebo, P., Schneider, B. Redesigning protein cavities as a strategy for increasing affinity in protein-protein interaction. Interferon-γ receptor 1 as a model. BioMed Research International (2015) ID 716945. doi: 10.1155/2015/716945. eISSN 2314-6141.

Charnavets, T., Nunvar, J., Necasova, I., Volker, J., Breslauer, K. J., Schneider, B. Conformational diversity of single-stranded DNA from bacterial repetitive extragenic palindromes: Implications for the DNA recognition elements of transposases. Biopolymers (2015) 103(10): 585-596. doi: 10.1002/bip.22666. EISSN 1097-0282.

Schneider, B., Cerny, J., Cech, P., Svozil, D., Gelly, J.-Ch., de Brevern, A. G. Bioinformatic analysis of the protein/DNA interface. Nucleic Acids Research (2014) 42: 3381-3394. doi: 10.1093/nar/gkt1273. ISSN 0305-1048.

Cech, P., Kukal, J., Cerny, J., Schneider, B., Svozil, D.  Automatic workflow for the classification of local DNA conformations. BMC Bioinformatics (2013) 14: 205. doi: 10.1186/1471-2105-14-205. ISSN 1471-2105.

Mikulecky, P., Cerny, J., Biedermannova, L., Petrokova, H., Kuchar, M., Vondrasek, J., Maly, P., Sebo, P., Schneider, B. Increasing affinity of interferon-γ receptor 1 to interferon-γ by computer-aided design. BioMed Research International (2013)  ID 752514. doi:10.1155/2013/752514.

Group Profile (Home Institution)

Contacts

Biotechnologický ústav AV ČR, v.v.i. (BIOCEV)
Průmyslová 595
252 50 Vestec
Česká republika
+420 325 873 700