Guía DocenteCurso Facultade de Ciencias |
Mestrado Universitario en Bioloxía Molecular , Celular e Xenética |
Asignaturas |
Dinámica e Estructura de Proteínas |
Fontes de información |
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Datos Identificativos | 2015/16 | |||||||||||||
Asignatura | Dinámica e Estructura de Proteínas | Código | 610441011 | |||||||||||
Titulación |
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Descriptores | Ciclo | Período | Curso | Tipo | Créditos | |||||||||
Mestrado Oficial | 2º cuadrimestre |
Primeiro | Optativa | 3 | ||||||||||
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Bibliografía básica | |
· Banaszak, L. J. (2000). Foundations of structural biology. Academic Press. · Berg, J. M., Tymoczko, J. L., Stryer. L. (2003). BIOQUÍMICA. 5ª Edición. Reverté. ·
Branden,
C. & Tooze, J. (1998). INTRODUCTION TO PROTEIN STRUCTURE. 2nd edition
Garland Publishing, Inc, · Cerdán Villanueva, M. E. (2005). Curso avanzado de proteínas y ácidos nucleicos. Universidade da Coruña. ·
Creighton,
T. E. (1993). PROTEINS: STRUCTURES AND MOLECULAR PROPERTIES, 2nd edition. W.H.
Freeman & Company, ·
Gómez-Moreno,
C. & Sancho, J. (Coords). (2003). ESTRUCTURA DE PROTEÍNAS. Ariel Ciencia, ·
Lesk, A.
M. (2000). INTRODUCTION TO PROTEIN ARCHITECTURE. THE STRUCTURAL BIOLOGY OF
PROTEINS. · Nelson, D. L., Cox, M. M. (2000). LEHNINGER PRINCIPLES OF BIOCHEMISTRY. Worth Publishers. Rodes, G. (2000). Crystallography. Made Crystal Clear. Academic Press. |
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Bibliografía complementaria | |
§ Carter, Jr., C.V. y Sweet, R. M. (1997). Macromolecular Crystallography, parts A and B. Methods in Enzymology, vols. 276 y 277. Academic Press. NY. §
Casari, G., Sander, C., § Clore, G. M. y Gonenborg, A. M. (1998). New methods of structure refinement for macromolecular structure determination by NMR. Proc. Natl. Acad. Sci., 95, 58915898. § Del Sol Mesa, A., Pazos, F., Valencia, A. (2003). Automatic methods for predicting functionally important residues. J. Mol. Biol., 326: 12891302. §
Ducruix, A., Giegé, R. (1999). Crystallisation of Nucleic Acids and
Proteins. A Practical Approach, edn 2. § Eyrich, V. A., MartiRenom, M. A., Przybylski, D., Madhusudhan, M.S., Fiser, A., Pazos, F., Valencia, A., Sali, A. y Rost, B. (2001). EVA: continuos automatic evaluation of protein structure prediction servers. Bioinformatics, 17: 12421243. § Ferentz, A.E. y Wagner, G. (2000). NMR spectroscopy: a multifaceted approach to macromolecular structure. Quarter Rev. Biophys. 33, 2965. § Fersht, A. R. (1999). Structure and Mechanism in Protein Science, Freeman and Co., NY. § Frank, J. (1996). Three dimensional electron microscopy of macromolecular assemblies. Academic Press, San Diego. §
Harris,
E. L. V. y Angel, S. (eds.) (1999): Protein purification methods. A practical
approach. IRL Press. §
James, T. L., Dötsch, V. y Smith, U. (2001). Nuclear Magnetic Resonante of Biological
Macromolecules. Part A and B. Methods Enzymol., 338, Academic Press, §
Juan, D.,
Graña, O., Pazos, F., Fariselli, P., Casadio, R., §
Kleanthous,
C. (ed.) (2000). ProteinProtein Recognition. § Mayo, K. H. y Daragan, U. A. (2003). Protein dynamics using NMR relaxation. World Scientific, Nueva Jersey. § McEwen, B. F. y Marcko, M. (2001). The emergente of electrón tomography as an important tool for investigating cellular ultrastructure. J. Histochem. Cytochem. Vol 49, 553563. § Mc Pherson, A. (2002). Introduction to Macromolecular Crystallography. John Wiley and Sons. Inc., NY.
§ Naomi, E. C. (2004). Turning Protein crystallisation from an art into a science. Current Opinion in Structural Biology, 14: 577583. § Sinha, N. y SmithGill, S. J. (2002). Protein structure to function via dynamics. Protein Peptid Letters, 9: 367377. § Van Heel, M. (2000). Single particle electrón cryomicroscopy: towards atomic resolution. Q. Rev. Byophis. Vol. 33, 307369. §
Igor Stagljar
and § Dobrin Nedelkov and Randall W. Nelson (2003) Surface plasmon resonance mass spectrometry: recent progress and outlooks • REVIEW . Trends in Biotechnology, 21: 301-305. §
Coordenadas: Protein Data Bank: http://www.rcsb.org/pdb BioMagResBank: http://www.brmb.wisc.edu Cambridge Crystall Data Centre: http://www.ccdc.cam.ac.uk Molecular Modelling DataBase: http://www.ncbi.nlm.nih.gov/structure Nucleic Acid Database: http://ndbserver.rutgers.edu:80/ MOOSE: http://db2.sdsc.edu/moose Molecules To Go ('R US): http://molbio.info.nih.gov/cgi-bin/pdb Enzyme Structures Database: http://www.ebi.ac.uk/thornton-srv/databases/enzymes Clasificación estructural CATH http://www.biochem.ucl.ac.uk/bsm/cath SCOP http://scop.mrc-lmb.cam.ac.uk/scop FSSP http://www2.embl-ebi.ac.uk/dali/fssp
Programas de visualización molecular: Rasmol: http://www.umass.edu/microbio/rasmol Swiss-PdbViewer: http://www.expasy.ch/spdbv/ MOLMOL http://www.mol.biol.ethz.ch/wuthrich/software/molmol Cn3D http://www.ncbi.nlm.nih.gov/Structure/CN3D/cn3d.shtml Chime http://www.umass.edu/microbio/chime Servidores de alineamientos de secuencias: BLAST http://www.ncbi.nlm.nih.gov/BLAST FASTA http://www.ebi.ac.uk/fasta33 Servidores de predicción y modelización:
SWISS-MODEL http://expasy.ch/swissmod/ The PredictProtein Server http://ww.embl-heidelberg.de/predictprotein/predictprotein.html Center for Molecular Modeling: http://cmm.info.nih.gov/modeling/ GRAMM: http://reco3.musc.edu/gramm/ PQS (Probable Quat. Structure): http://msd.ebi.ac.uk/services/quaternary/quaternary.html |
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