Bibliografía:

         General

        Hélices a 

•    general

• Stability of a-helices. Chakrabartty A & Baldwin RL. Advances in Protein Chemistry 46: 141-176 (1995).

•     posiciones internas

• Conformational parameters for amino acids in helical, b-sheet, and random coil regions calculated from proteins. Chou PY & Fasman GD. Biochemistry 13: 211-222 (1974)

• a-Helix stability in protein. II. Factors that influence stability at an internal position. Horovitz A, Matthews JM & Fersht AR. J. Mol. Biol. 227: 560-568 (1992).

•     caps

• Amino acid preferences for specific locations at the ends of a-helices. Richardson J.S. & Richardson, D.C. Science 240:1648-1652 (1988)

• a-helix stability in proteins. I. Empirical correlations concerning substitutions of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent exposed surfaces. Serrano, L., Sancho, J. Hirshberg, M & Fersht, A.

• N- and C-capping preferences for all 20 amino acids in a-helical peptides. Doig AJ & Baldwin RL. Prot. Sci. 4: 1325-1336 (1995).

•     señales de terminación

• Helix signals in proteins. Presta, L.G. & Rose G.D. Science 240: 1632-1641 (1988)

• Sequence determinats of the capping box, a stabilizing motif at the N-termini of a-helices. Seale, J.W., Srinivasan, R. & Rose, G.D. Protein Science 3, 1741-1745 (1994)

• Rules for a-helix termination by glycine. Aurora R, Srinivasan R & Rose GD.Science 264: 1126-1130 (1994).

• Helix stop signals in proteins and peptides: the capping box. Harper ET & Rose GD.Biochemistry 32: 7605-7609 (1993).

•     interacciones entre cadenas

• Intrahelical side chain interaction in a-helices: poor correlation between energetics and frequency. J. Fernández-Recio & J. Sancho. FEBS Letters 429: 99-103 (1998

• Ion-pair and charged hydrogen-bond interactions between histidine and aspartate in a peptide helix. Huyghues-Despointes BMP & Baldwin RL. Biochemistry 36: 1965-1970 (1997).

• The tryptophan/histidine interaction in a-helices. J. Fernández-Recio, A. Vázquez, C. Civera, P. Sevilla & J. Sancho. J. Mol. Biol. 267: 184-197 (1997)

• AGADIR

• Muñoz V & Serrano L. 1994. Elucidating the folding problem of helical peptides using empirical parameters. Nature. Structural Biology 1: 399-409.

• Thermodynamic b-sheet propensities measured using a zinc-finger host peptide. CA Kim, JM Berg. Nature 362: 267-270 (1993)

• Context is a major determinant of b-sheet propensity. Minor, D.L.Jr., Kim, P.S. Nature, 371, 264-267 (1994)

• Measurement of the b-sheet-forming propensities of amino acids. DL Minor, PS Kim 367:660-663 (1994)

• A thermodynamic scale for the b-sheet forming tendencies of the amino acids. CK Smith, JM Withka, & L Regan. Biochem. 33:5510-5517 (1995).

• Guidelines for protein design: the energetics of b-sheet side chain interactions. Smith CK & Regan L. Science 270: 980-982 (1995).

• Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices. Comparison with experimental scales. V Muñoz & L Serrano. Proteins 20:301-311 (1994)

• Side-chain determinants of b-sheet stability. DE Otzen & AR Ferhst. Biochemistry 34:5718-5724 (1995).

• Cross-strand side chain interactions versus turn conformations in b-hairpins. E De Alba, M Rico, MA Jiménez. Prot Sci 6:2548-2560 (1997).

• Structural principles of a/b barrel proteins:: the packing of the interior of the sheet. Lesk, A. M., Bränden ,C-I & Chothia, C.Proteins: structure, function and genetics. 5:139-148 (1989)

• Conformation of b-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering. Sibanda, B.L., Blundell, T.L. & Thorton, J.M. J. Mol. Biol. 206: 759-777 (1989)

• Folding dynamics and mechanism of b-hairpin formation. V Muñoz, PA Thompson, J Hofrichter, WA Eaton. Nature 390:196-199 (1997).

• De novo design and structural analysis of a model b-hairpin peptide system. M Ramirez-Alvarado, FJ Blanco, L Serrano. Nat. Struct. Biol. 3:604-612 (1996).