Teaching GuideTerm
Faculty of Science
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Mestrado Universitario en Bioloxía Molecular , Celular e Xenética
 Asignaturas
  Dinámica e Estructura de Proteínas
   Fontes de información
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, New York.

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, New York.

Gómez-Moreno, C. & Sancho, J. (Coords). (2003). ESTRUCTURA DE PROTEÍNAS. Ariel Ciencia, Barcelona.

Lesk, A. M. (2000). INTRODUCTION TO PROTEIN ARCHITECTURE. THE STRUCTURAL BIOLOGY OF PROTEINS. Oxford University Press, Oxford.

Nelson, D. L., Cox, M. M. (2000). LEHNINGER PRINCIPLES OF BIOCHEMISTRY. Worth Publishers.

Rodes, G. (2000). Crystallography. Made Crystal Clear. Academic Press.

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., Valencia, A. (1995). A method to predict functional residues in proteins. Nature Struct. Biol., 2: 171178.

§ 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. Oxford University Press. Oxford.

§ 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. Oxford.

§ James, T. L., Dötsch, V. y Smith, U. (2001). Nuclear Magnetic Resonante of Biological Macromolecules. Part A and B. Methods Enzymol., 338, Academic Press, San Diego.

§ Juan, D., Graña, O., Pazos, F., Fariselli, P., Casadio, R., Valencia, A. (2003). A neural network approach to evaluate Fold recognition results. Proteins Mar 1,(4): 50, 600608.

§ Kleanthous, C. (ed.) (2000). ProteinProtein Recognition. Oxford University Press, Oxford.

§ 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 Stanley Fields (2002). Analysis of membrane protein interactions using yeast-based technologies • REVIEW . Trends in Biochemical Sciences, 27: 559-563.

§ Sandor Vajda and Carlos J. Camacho (2004). Protein–protein docking: is the glass half-full or half-empty? Trends in Biotechnology, 22: 110-116.

§ Dobrin Nedelkov and Randall W. Nelson (2003). Surface plasmon resonance mass spectrometry: recent progress and outlooks • REVIEW Trends in Biotechnology, 21: 301-305.

§ Takashi Ito, Tomoko Chiba and Mikio Yoshida (2001). Exploring the protein interactome using comprehensive two-hybrid projects • REVIEW . Trends in Biotechnology, 19 (Supplement 1): 23-27.

§ Valerio Orlando (2000). Mapping chromosomal proteins in vivo by formaldehyde-crosslinked-chromatin immunoprecipitation • REVIEW . Trends in Biochemical Sciences, 25: 99-104.

§ Dobrin Nedelkov and Randall W. Nelson (2003) Surface plasmon resonance mass spectrometry: recent progress and outlooks • REVIEW . Trends in Biotechnology, 21: 301-305.

§ Philippe I. H. Bastiaens and Rainer Pepperkok (2000). Observing proteins in their natural habitat: the living cell • REVIEW . Trends in Biochemical Sciences, 25: 631-637

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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