Předmět: Biomolecular Structures ? Determination and Characterization

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Název předmětu Biomolecular Structures ? Determination and Characterization
Kód předmětu UCH/027
Organizační forma výuky Přednáška + Cvičení
Úroveň předmětu Doktorský
Rok studia nespecifikován
Četnost výuky V každém akademickém roce, jen v zimním semestru.
Semestr Zimní
Počet ECTS kreditů 4
Vyučovací jazyk angličtina
Statut předmětu Povinně-volitelný
Způsob výuky Kontaktní
Studijní praxe Nejedná se o pracovní stáž
Doporučené volitelné součásti programu Není
Vyučující
  • Pavlíček Jiří, RNDr. Ph.D.
  • Biedermannová Lada, RNDr. Ph.D.
  • Schneider Bohdan, prof. Ing. CSc., DSc.
Obsah předmětu
One week course at the Institute of Biotechnology of the Czech Academy of Sciences, usually in the first or second week of January. Introduction to crystallography as the most important method of determination of molecular structures. Why study molecular structures, structure-function relationships in chemistry and biology? Experimental setup, crystal growth, sources of radiation (x-ray lamps, synchrotron etc.) Data collection and reduction. Crystallographic symmetry Structure determination. Solution of the phase problem? Reflections, electron densities and Fourier transforms Structure refinement. Improvement of the molecular model Validation and analysis of structures Comparison of crystallography to other experimental methods as electron microscopy, NMR, and other spectral methods, and to methods of computer simulations by quantum mechanics and methods of empirical potential (molecular dynamics). Finding structures: Structural databases. Practical introduction to the most important databases CSD (for organic molecules) and PDB (the primary repository for 3-D macromolecular structures). Other internet databases important for structural biology. mmCIF and other formats used for archiving structures Comparing structures by tools of structural bioinformatics. Stereochemistry of the building blocks of biomolecules, amino acids and nucleotides. Sequence alignments, relationship between amino acid sequence and protein structure and fold. Methods of structure comparisons. Structural motives of the protein secondary structure, tertiary structure motives, classifications of protein folds. Structures of nucleic acids. I. Helical conformations. II. 3D folding of RNA and DNA.

Studijní aktivity a metody výuky
Monologická (výklad, přednáška, instruktáž), Dialogická (diskuze, rozhovor, brainstorming), Exkurze
  • Účast na výuce - 39 hodin za semestr
  • Exkurze - 6 hodin za semestr
  • Příprava na zkoušku - 25 hodin za semestr
  • Domácí příprava na výuku - 30 hodin za semestr
Výstupy z učení
Introduction to crystallography as the most important method of determination of molecular structures. Why study molecular structures, structure ? function relationships in chemistry and biology Experimental setup, crystal growth, sources of radiation (x-ray lamps, synchrotron etc.) Data collection and reduction. Crystallographic symmetry Structure determination. Solution of the ?phase problem? Reflections, electron densities and Fourier transforms Structure refinement. Improvement of the molecular model Validation and analysis of structures Comparison of crystallography to other experimental methods as electron microscopy, NMR, and other spectral methods, and to methods of computer simulations by quantum mechanics and methods of empirical potential (molecular dynamics). Finding structures: Structural databases. Practical introduction to the most important databases CSD (for organic molecules) and PDB (the primary repository for 3-D macromolecular structures). Other internet databases important for structural biology. mmCIF and other formats used for archiving structures Comparing structures by tools of structural bioinformatics. Stereochemistry of the building blocks of biomolecules, amino acids and nucleotides. Sequence alignments, relationship between amino acid sequence and protein structure and fold. Methods of structure comparisons. Structural motives of the protein secondary structure, tertiary structure motives, classifications of protein folds. Structures of nucleic acids. I. Helical conformations. II. 3D folding of RNA and DNA.
Students gain a basic knowledge of structural biochemistry and X-ray crystallography. Practical part takes places at the Institute of Biotechnology of the Czech Academy of Sciences.
Předpoklady
Knowledge of biochemistry, organic chemistry, molecular biology is expected.

Hodnoticí metody a kritéria
Kombinovaná zkouška

Student musí porozumět vyučovanému obsahu v teoretické i praktické rovině a aktivně se účastnit práce na cvičeních. K získání zkoušky musí obdržet alespoň 50% bodů.
Doporučená literatura
  • A.M. Lesk: Introduction to Bioinformatics. Oxford University, Oxford (2002).
  • B. Alberts; A. Johnson; J. Lewis; M. Raff; K. Roberts; P. Walter: Molecular Biology of the Cell, Garland, New York.
  • C. Brandén & J. Tooze: Introduction to Protein Structure. Second Edition, Garland, New York (1998).
  • G. Rhodes: Crystallography made crystal clear. Elsevier, Amsterdam (2006).
  • J. Drenth: Principles of protein x-ray crystallography. Springer, New York (1994).
  • J. Gu & P.E. Bourne: Structural Bioinformatics. Second Edition, Wiley-Blackwell, Hoboken (2009).
  • J.P. Glusker; M. Lewis; M. Rossi: Crystal Structure Analysis for Chemists and Biologists. VCH, New York (1994).
  • S. Neidle: Nucleic acid structure and recognition, Oxford University, Oxford (2002).


Studijní plány, ve kterých se předmět nachází
Fakulta Studijní plán (Verze) Kategorie studijního oboru/specializace Doporučený ročník Doporučený semestr