“termodinámica y cinética del plegamiento

Curso Fundamental

 

 

Bibliografía GENERAL.

 

 

Alberty, R. A., Silbey, R. J. (1997) Physical Chemistry. Wiley, USA.

 

Branden C. y Tooze J. (1999) Introduction to Protein Structure. Ed. Garland Publishing, Inc,. New York, USA.

 

Bergethon, P.R. (1998) The physical basis of biochemistry. Springer-Verlag, USA.

 

Bogan, A. A. & Thorn, K.S. (1998) An analysis of hot spots in protein interfaces. J. Mol. Biol. 280, 1-9.

 

Chotia, C. & Janin, J. (1975) Principles of protein-protein recognition. Nature, 256: 705-708.

 

Creigthon, T.E.  Ed.  (1992). Protein Folding. Freeman. USA.

 

Dill, KA, Chan, HS (1997) From Levinthal to pathways to funnels. Nature Struct Biol. 4:10-19.

 

Eisenberg, D. y Crothers, (1979). Physical Chemistry. The Benjamin/Cummings Publishing Company. USA.

 

Fersht, A.R. (1999).  Structure and mechanism in protein science. Freeman. USA.

Hilser, VJ, Dowdy, D, Oas, TG, Freire, E (1998) The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. Proc Natl Acad Sci USA 95:9903-9908.

 

Jacob, M. y F. X. Schmid, (1999). Protein Folding as a Diffusional Process. Biochem 38, 13773-13779.

 

Karplus, M. y D. L. Weaver, (1994). Protein Folding Dynamics: The Diffusion-collision Model and Experimental Data. Protein Sci 3, 650-668.

 

Lazaridis, T, Archontis, G, Karplus, M (1995) Enthalpic contribution to protein stability: insights from atom-based calculations and statistical mechanics. Adv Protein Chem 47:231-306.

 

Luque, I, Gómez, J, Semo, N, Freire, E (1998) Structure-based thermodynamic design of peptide ligands: application to peptide inhibitors of the aspartic protease endothiapepsis. Proteins: Struct Funct Genet 30:74-85.

 

Makhatadze, GI, Privalov, PL (1995) Energetics of protein structure. Adv Protein Chem 47: 307-425.

 

Matthews, CR Ed. (2000) Protein folding mechanisms. Adv Protein Chem 53.

 

Nozaki, Y., Tanford, C. (1971) The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. J. Biol. Chem. 246, 2211-2217.

 

Plaxco, K. W. y D. Baker, (1998). Limited Internal Friction in the Rate-limiting Step of a Two-state Protein Folding Reaction. Proc Natl Acad Sci USA 95, 13591-13596.

 

Plticelli, F, Ascenzi, P, Bolognesi, M, Honig, B (1999) Structural determinants of trypsin affinity and specificity for cationic inhibitors. Protein Sci 8:2621-2629.

 

Steinfeld, J. F., Francisco J. S. y Hase, W. L. (1989). Chemical Kinetics and Dynamics. Prentice Hall. USA.

 

Tinoco, I., K. Sauer y J. C. Wang, (1995). Physical Chemistry. 3ª edición, Prentice Hall. USA.

 

Weber, G. (1992) Protein Interactions. Chapman & Hall. USA.

Zhou, Y, Hall, CK, Karplus, M (1999) The calorimetric criterion for a two-state process revisited. Protein Sci 8:1064-1074.

 

 

 

REGRESA  A PÁGINA PRINCIPAL

Justificación

Lugar y duración

Evaluación

Responsables del curso

 

 

 

 

 

sugerencias o comentarios sobre esta página:

 

 

evazquez@bq.unam.mx

 

 

 

Visita la página de la Rama de FISICOQUÍMICA, ESTRUCTURA Y DISEÑO DE PROTEÍNAS de la SMB

 

.