Applied Pharmaceutical Structural Bioinformatics (GK 301) aims to teach how to solve practical problems in pharmacology, life sciences. Course includes methods, databases and software for analysis and management of amino acid and nucleotide sequences, secondary and tertiary structures of proteins. Focus is on practical exercises where the student solves biophysical structural problem.
Applied Pharmaceutical Structural Bioinformatics (GK 301) aims to teach how to solve practical problems in pharmacology, life sciences. Course includes methods, databases and software for analysis and management of amino acid and nucleotide sequences, secondary and tertiary structures of proteins. Focus is on practical exercises where the student solves biophysical structural problem.
Applied Pharmaceutical Structural Bioinformatics (GK 301) aims to teach how to solve practical problems in pharmacology, life sciences. Course includes methods, databases and software for analysis and management of amino acid and nucleotide sequences, secondary and tertiary structures of proteins. Focus is on practical exercises where the student solves biophysical structural problem.
Duration: Flexible 10 weeks Location for Studies: Flexible (Onsite preferred) Outline of the course: The course is given through down-loadable documents, audio-visual selfstudies and teacher-supervised exercises that student solves on computer using available software. The course has no fixed times and the student can carry out their duties at any time of each study week. This course on Applied Pharmaceutical Structural Bioinformatics intends to teach how to solve practical problems in pharmacology, life sciences and bioinformatics of your molecule of interest using free software and databases relating to the structure of functional proteins and drug targets. The course covers bioinformatics for nucleotide and amino acid sequences and structural bioinformatics. This includes methods, databases and software for analysis and management of amino acid and nucleotide sequences, secondary and tertiary structures of proteins, methods and tools for homology modeling of protein 3D structure, and molecular dynamics simulations and molecular docking. The focus of the course is on practical exercises where the student solves biophysical structural problem. Besides theoretical teachings, course contains the following practical sections:
Data base searching
Pairwise and multiple sequence alignments Prediction of secondary protein structure Prediction of protein 3D structure 3D Structure Visualization (PyMol) Validation of 3D structures Molecular dynamic simulation Molecular docking and drug screening (computer-aided drug design) Generate publication quality images and videos Build a web page that shows your study research report Compile and submit your results to a journal for publication