Lecturas obligatorias

Life's Matrix, Philip Ball, University of California Press, 2001.

Christopher K. Matthews & K.E. Van Holde, Biochemistry, 2.ª edición. Benjamin Cummings Publishing Company, Menlo Park, CA., 1996.

Aminoácidos

Lubert Stryer, Biochemistry 4.ª  ed., W. H. Freeman & Co. Nueva York, 1995; traducción española de Macarulla, Jose María, Bioquímica. Barcelona. Editorial Reverté.

Geoffrey Zubay, Biochemistry, 3.ª  ed., W C. Brown Publishers, Oxford, UK, 1993.

Christopher K. Matthews & K.E. Van Holde, Biochemistry, 2.ª edición, Benjamin Cummings Publishing Company, Menlo Park, CA, 1996.

Carl Branden & John Tooze, Introduction to Protein Structure, Garland Publishing, Inc., Nueva York, 1999.

Thomas Creighton, Proteins, Structures and Molecular Properties, W. H. Freeman & Co., Nueva York, 1993.

Estructuras primaria y secundaria de las proteínas

The Structure and Action of Proteins, Richard Dickerson, editorial Harper & Row Publishers, Nueva York, 1969.

The Nature of Chemical Bond: Structural Properties, 2.ª edición, Linus Pauling, editorial Cornell University Press, Nueva York, 1960.

Introduction to Protein Structure. Carl Branden & John Tooze, editorial Garland Publishing, Inc., Nueva York, 1999.

Proteins, Structures and Molecular Properties. Thomas Creighton, editorial W. H. Freeman & Co. Nueva York, 1993.

Hélices

The Structure and Action of Proteins, Richard Dickerson, 1969.

The Nature of Chemical Bond: Structural Properties, 2nd Ed., Linus Pauling, editorial Cornell University Press, Nueva York, 1960.

Branden, Carl & John Tooze, Introduction to Protein Structure. Editorial Garland Publishing, Inc., Nueva York, 1999.

Thomas Creighton, Proteins, Structures and Molecular Properties. Editorial W. H. Freeman & Co. Nueva York, 1993.

Fancis Crick. The packing of a-helices: Simple Coiled-Coils. Acta. Cryst. 1953. Cap. 6, págs. 689-697.

O'Shea E.K., Klemm J.D., Kim P.S., Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil.  Science. 1991, 254:539-44.

Lovejoy B., Choe S., Cascio D., McRorie D.K., DeGrado W.F., Eisenberg D. Crystal structure of a synthetic triple-stranded alpha-helical bundle.  Science. 1993, 259:1288-93.

Lumb KJ, Kim PS. Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science. 1995, 268:436-9.

Kohn WD, Mant CT, Hodges RS. Alpha-helical protein assembly motifs.  J Biol Chem. 1997, 272:2583-6. Review.

Láminas beta 

Pauling, Linus y Robert B. Corey. The pleated sheet, a new layer configuration of polypeptide chains. PNAS. May 15, 1951. 37, 251-256.

Pauling, Linus and Robert B. Corey.  Configurations of polypeptide chains with favored orientations around single bonds: two new pleated sheets.  PNAS. May 15, 1951. Vol 37, No. 5.  729-740.

Cristalografía de rayos X

Branden, Carl y John Tooze, Introduction to Protein Structure. Editorial Garland Publishing, Inc., Nueva York, 1999.

Creighton, Thomas, Proteins, Structures and Molecular Properties. Editorial W. H. Freeman & Co. Nueva York, 1993.

NMR

Branden, Carl y John Tooze, Introduction to Protein Structure. Editorial Garland Publishing, Inc., Nueva York, 1999.

Creighton, Thomas, Proteins, Structures and Molecular Properties. Editorial W. H. Freeman & Co. Nueva York, 1993.

Herramientas utilizadas en el estudios y en el análisis de estructuras moleculares (II): dicroismo magnético circular, técnica Raman, FTIR, AFM, TEM, SEM, dispersión de luz

Branden, Carl y John Tooze, Introduction to Protein Structure. Editorial Garland Publishing, Inc., Nueva York, 1999.

Creighton, Thomas, Proteins, Structures and Molecular Properties. Editorial W. H. Freeman & Co. Nueva York, 1993.

Transición: estructura molecular de otras proteínas fibrosas

Branden, Carl y John Tooze, Introduction to Protein Structure. Editorial Garland Publishing, Inc., Nueva York, 1999.

Creighton, Thomas, Proteins, Structures and Molecular Properties. Editorial W. H. Freeman & Co. Nueva York, 1993.

Estructura molecular del colágeno

The Extracellular Matrix Factsbook, 2nd Ed., Shirley Ayad, et al, editorial AP Factsbooks, San Diego, CA, 1998.

Extracellular Matrix Assembly & Structure, Peter Yurchenco, et al., AP, San Diego, CA, ed. 1994.

Treaties on Collagen, G. N. Ramachandran, AP, San Diego, CA, ed. 1967.

Pauling, Linus y Robert B. Corey.  The structure of fibrous proteins of the collagen-gelatin group.  PNAS. Vol 37, 272-281, 1951.

John Highberger, Jerome Gross, Francis Schmitt.  The Interaction of Microportein with Soluble collagen; and Electron Microscope Study. PNAS. Vol 37: 286-293, 1951.

Alexander Rich y Francis Crick. The Structure of Collagen. Nature. Vol 176, págs. 915-916, 1955.

Rich A.  Follow that fiber. Nat Struct Biol. 5(8)675, agosto 1998.

Rich A. Chasing collagen. Nat Struct Biol. 5(9)760, septiembre 1998.

Rich A. Structure of collagen. Nat Struct Biol. 5(10)858-9, octubre 1998.

Bella J., Eaton M., Brodsky B., Berman H.M. Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution. Science. 266(5182):75-81, 7 de octubre de 1994.

Bella J, Brodsky B, Berman HM. Hydration structure of a collagen peptide. Structure. 3(9):893-906, 15 de septiembre de 1995.

Kramer RZ, Bella J, Brodsky B, Berman HM. The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence. J Mol Biol. 311(1):131-47, 3 de agosto de 2001.

Engel J, Prockop DJ. Does bound water contribute to the stability of collagen? Matrix Biol. 17(8-9):679-80, diciembre 1998

Linus Pauling and Robert B. Corey. The structure of feather Rachis keratin.  PNAS. Vol 37, No. 5. 256-261, 15 de mayo de 1951.

Seda

Silk Polymers: Materials Science & Biotechnology, David Kaplan, Wade Adams, Barry Farmer y Christopher Viney, redactores, ACS Sympoisum Series 544, 1993.

Van Beek J.D., Beaulieu L., Schafer H., Demura M., Asakura T., Meier BH. Solid-state NMR determination of the secondary structure of Samia cynthia ricini silk.  Nature. 405(6790):1077-9, 29 de junio de 2000.

Tirrell DA. Putting a new spin on spider silk. Science. 271(5245):39-40, 5 de enero de 1996.

Hayashi CY, Lewis RV. Molecular architecture and evolution of a modular spider silk protein gene. Science. 287(5457):1477-9, 25 de febrero de 2000.

Hayashi CY, Lewis RV. Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks.  J Mol Biol. 275(5):773-84, 6 de febrero de 1998.

Mita K, Ichimura S, Zama M, James TC. Specific codon usage pattern and its implications on the secondary structure of silk fibroin mRNA. J Mol Biol. 203 (4):917-25, 20 de octubre de 1988.

Mori S, Izumi S, Tomino S. Structures and organization of major plasma protein genes of the silkworm Bombyx mori. J Mol Biol. 218(1):7-12, 5 de marzo de 1991.

Valluzzi R, Winkler S, Wilson D, Kaplan DL. Silk: molecular organization and control of assembly. Philos Trans R Soc Lond B Biol Sci. 357(1418):165-7, febrero de 2002.

Regenerated Spider Silk: Processing, Properties, and Structure.  Seidel, A.; Liivak, O.; Calve, S.; Adaska, J.; Ji, G.; Yang, Z.; Grubb, D.; Zax, D. B.; Jelinski, L. W.; Macromolecules. 33(3); 775-780, 2000.

Biominerales I: conchas y diatomeas

Biomineralization, Stephen Mann, redactor, VCH Publishers, Inc, 1996.

Biomineralization: Cell Biology &Mineral Deposition, Kenneth Simkies & Karl Wilbur, Academic Press, San Diego, CA, 1989.

Richard Frankel y Richard Blackmore, redactores, Iron Biominerals, Plenum Press, Nueva York, 1991.

Shimizu K, Cha J, Stucky GD, Morse DE. Silicatein alpha: cathepsin L-like protein in sponge biosilica. Proc Natl Acad Sci U S A. 95:6234-8, 1998.

Cha JN, Shimizu K, Zhou Y, Christiansen SC, Chmelka BF, Stucky GD, Morse DE. Silicatein filaments and subunits from a marine sponge direct the polymerization of silica and silicones in vitro. Proc Natl Acad Sci U S A. 96:361-5, 1999.

Aizenberg J, Tkachenko A, Weiner S, Addadi L, Hendler G. Calcitic microlenses as part of the photoreceptor system in brittlestars.  Nature. 412:819-22, 2001.

Control of Aragonite or Calcite Polymorphism by Mollusk Shell Macromolecules Giuseppe Falini, Shira Albeck, Steve Weiner y Lia Addadi, Science. 271: 67-69, 1996.

Biominerales II: huesos y dientes

Weiner S, Veis A, Beniash E, Arad T, Dillon JW, Sabsay B, Siddiqui F. Peritubular dentin formation: crystal organization and the macromolecular constituents in human teeth. J Struct Biol. 126(1):27-41, 1 de junio de 1999.

Wang RZ, Weiner S. Strain-structure relations in human teeth using Moire fringes.  J Biomech. 31(2):135-41, 1998.

Weiner S, Traub W, Wagner HD. Lamellar bone: structure-function relations. J Struct Biol. 126(3):241-55, 1999.

Wang R, Weiner S. Human root dentin: structural anisotropy and Vickers microhardness isotropy. Connect Tissue Res. 39(4):269-79, 1998.

S. Weiner and H. D. Wagner, THE MATERIAL BONE: Structure-Mechanical Function Relations. Annu. Rev. Mater. Sci. Vol. 28: 271-298, 1998.

Estructura de las diatomeas

Biomimetics: Design and Processing of Materials, Mehmet Sarikaya & Ilhan Aksay, redactores, AIP Series, Nueva York, 1995.

Kroger N, Deutzmann R, Sumper M. Polycationic peptides from diatom biosilica that direct silica nanosphere formation. Science. 286:1129-32, 1999.

Kroger N, Bergsdorf C, Sumper M. Frustulins: domain conservation in a protein family associated with diatom cell walls. Eur J Biochem. 239:259-64, 1996.

Kroger N, Lehmann G, Rachel R, Sumper M. Characterization of a 200-kDa diatom protein that is specifically associated with a silica-based substructure of the cell wall. Eur J Biochem. 250:99-105, 1997.

Kroger N, Bergsdorf C, Sumper M. A new calcium binding glycoprotein family constitutes a major diatom cell wall component. EMBO J. 13:4676-83, 1994.

Kroger N, Deutzmann R, Sumper M. Silica-precipitating peptides from diatoms. The chemical structure of silaffin-A from Cylindrotheca fusiformis. J Biol Chem. 276:26066-70, 2001.

Estructura molecular del ADN y el ARN

Watson JD, Crick FH. Molecular structure of nucleic acids: a structure for deoxyribose nucleic acid. Nature, number 4356; 25 de abril de 1953.

Watson JD, Crick FH. Molecular structure of nucleic acids: a structure for deoxyribose nucleic acid. Nature; 248(451):765; 26 de abril de 1974.

Wang AH, Quigley GJ, Kolpak FJ, Crawford JL, van Boom JH, van der Marel G, Rich A. Molecular structure of a left-handed double helical DNA fragment at atomic resolution. Nature; 282(5740):680-6; 13 de diciembre de 1979.

Máquinas moleculares de ADN

Bethell D, Schiffrin DJ. Supramolecular chemistry. Nanotechnology and nucleotides. Nature; 382:581; 1996.

Schmidbaur H. Supramolecular chemistry. Going for gold. Nature, 413:31, 33; 2001.

Alivisatos AP, Johnsson KP, Peng X, Wilson TE, Loweth CJ, Bruchez MP Jr, Schultz PG. Organization of 'nanocrystal molecules' using DNA. Nature, 382:609-11; 1996.

Mao C, Sun W, Shen Z, Seeman NC. A nanomechanical device based on the B-Z transition of DNA. Nature; 397(6715):144-6, 14 de enero de 1999.

Yurke B, Turberfield AJ, Mills AP, Simmel FC, Neumann JL. A DNA-fuelled molecular machine made of DNA. Nature; 406:605-8, 2000.

Braun E, Eichen Y, Sivan U, Ben-Yoseph G. DNA-templated assembly and electrode attachment of a conducting silver wire. Nature: 391:775-8, 1998.

Winfree E, Liu F, Wenzler LA, Seeman NC. Design and self-assembly of two-dimensional DNA crystals. Nature; 394(6693):539-44, 6 de agosto de 1998.

Chen JH, Seeman NC. Synthesis from DNA of a molecule with the connectivity of a cube. Nature; 350:631-3; 1991.

Autoensamblaje de lípidos como materiales de construcción

Groves JT, Boxer SG, McConnell HM. Electric field-induced reorganization of two-component supported bilayer membranes Proc Natl Acad Sci U S A; 94:13390-5; 1997.

 Lvov, Y. M.; Price, R. R.; Selinger, J. V.; Singh, A.; Spector, M. S.; Schnur, J. M.; Langmuir; Imaging Nanoscale Patterns on Biologically Derived Microstructures; 16: 5932-5935; 2000.

Spector MS, Easwaran KR, Jyothi G, Selinger JV, Singh A, Schnur JM. Chiral molecular self-assembly of phospholipid tubules: a circular dichroism study. Proc Natl Acad Sci U S A; 93:12943-6; 1996.

Heyse S, Stora T, Schmid E, Lakey JH, Vogel H. Emerging techniques for investigating molecular interactions at lipid membranes. Biochim Biophys Acta; 1376(3):319-38; 10 de noviembre de 1998. Reseña. No existe resumen.

Aussillous P, Quere D. Liquid marbles. Nature; 411:924-7; 2001.

Mahadevan L. Non-stick water. Nature; 411:895-6; 2001.

Spector MS, Schnur JM. DNA ordering on a lipid membrane. Science; 275:791-2; 1997.

Sacáridos como materiales de construcción

Semino, CE. Saccharides as construction materials (transcripción en proceso).

The Living Colors ^TM - "Pintar una lata"

Yang F, Moss LG, Phillips GN Jr., The molecular structure of green fluorescent protein. Nat Biotechnol; 14:1246-51, 1996.

Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ. Crystal structure of the Aequorea victoria green fluorescent protein. Science, 273:1392-5; 1996.

Crameri A, Whitehorn EA, Tate E, Stemmer WP. Improved green fluorescent protein by molecular evolution using DNA shuffling.  Nat Biotechnol, 14:315-9; 1996.

Tsien RY. Rosy dawn for fluorescent proteins.  Nat Biotechnol; 17:956-7; 1999.

Matz MV, Fradkov AF, Labas YA, Savitsky AP, Zaraisky AG, Markelov ML, Lukyanov SA. Fluorescent proteins from nonbioluminescent Anthozoa species. Nat Biotechnol, 17:969-73; 1999.

Youvan DC, Michel-Beyerle ME. Structure and fluorescence mechanism of GFP. Nat Biotechnol, 14:1219-20; 1996.

Otros ejemplos de diseño de materiales biológicos

Urry DW. Elastic molecular machines in metabolism and soft-tissue restoration. Trends Biotechnol, 17:249-57; 1999.

Fernandez-Lopez S, Kim HS, Choi EC, Delgado M, Granja JR, Khasanov A, Kraehenbuehl K, Long G, Weinberger DA, Wilcoxen KM, Ghadiri MR.  Antibacterial agents based on the cyclic D,L-alpha-peptide architecture. Nature, 412:452-5; 2001.

Winfree E, Liu F, Wenzler LA, Seeman NC. Design and self-assembly of two-dimensional DNA crystals. Nature, 394:539-44; 1998

Aggeli A, Nyrkova IA, Bell M, Harding R, Carrick L, McLeish TC, Semenov AN, Boden N. Hierarchical self-assembly of chiral rod-like molecules as a model for peptide beta -sheet tapes, ribbons, fibrils, and fibers. Proc Natl Acad Sci U S A, 98:11857-62; 2001.

Xu G, Wang W, Groves JT, Hecht MH. Self-assembled monolayers from a designed combinatorial library of de novo beta-sheet proteins. Proc Natl Acad Sci U S A, 98:3652-7; 2001.

West MW, Wang W, Patterson J, Mancias JD, Beasley JR, Hecht MH. De novo amyloid proteins from designed combinatorial libraries. Proc Natl Acad Sci U S A, 96:11211-6; 1999.

Joel M. Schnur. Lipid Tubules: A Paradigm for Molecularly Engineered Structures, Science, 262:1669-1676; 1993.

Saghatelian A, Yokobayashi Y, Soltani K, Ghadiri MR. A chiroselective peptide replicator. Nature, 409:797-801; 2001.

Mihara H, Takahashi Y. Engineering peptides and proteins that undergo alpha-to-beta transitions. Curr Opin Struct Biol, 7:501-8; 1997.

Aggeli A, Bell M, Boden N, Keen JN, Knowles PF, McLeish TC, Pitkeathly M, Radford SE. Responsive gels formed by the spontaneous self-assembly of peptides into polymeric beta-sheet tapes. Nature, 386:259-62; 1997.

Yuta Takahashi, Akihiko Ueno, Hisakazu Mihara. Design of a Peptide Undergoing alpha - beta Structural Transition and Amyloid Fibrillogenesis by the Introduction of a Hydrophobic Defect, 4:2475-2484; 1998.

Hecht MH. De novo design of beta-sheet proteins. Proc Natl Acad Sci U S A, 91:8729-30; 1994.

Dobson CM. Protein misfolding, evolution and disease. Trends Biochem Sci, 24:329-32; 1999.

Urry, D. W.; Physical Chemistry of Biological Free Energy Transduction As Demonstrated by Elastic Protein-Based Polymers J. Phys. Chem. B; 101; 11007-11028; 1997.

Quinn TP, Tweedy NB, Williams RW, Richardson JS, Richardson DC. Betadoublet: de novo design, synthesis, and characterization of a beta-sandwich protein. Proc Natl Acad Sci U S A, 91:8747-51; 1994.