Máster Universitario en Bioloxía Molecular, Celular e Xenética (semipresencial) |
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Datos Identificativos | 2021/22 | |||||||||||||
Asignatura | Dinámica y Estructura de Proteínas | Código | 610441012s | |||||||||||
Titulación |
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Descriptores | Ciclo | Periodo | Curso | Tipo | Créditos | |||||||||
Máster Oficial | 2º cuatrimestre |
Primero | Optativa | 3 | ||||||||||
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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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Complementária | |
§ 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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