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Facultade de Ciencias
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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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