R-ficoeritrina de gracilaria chilensis: Estabilidad e interaction entre subunidades

Boletin de la Sociedad Chilena de Quimica

Volumn 45, Issue 2, 2000, Pages 303-309

  Bunster, Marta ^a   Contreras Martel, Carlos ^a   Bruna, Carola ^a   Oyanedel, José Martínez ^a  

^a Laboratorio de Biofîsica Molecular

Author keywords

Interaction surfaces; R phycoerythrin; Stability

Indexed keywords

EID: 23044517516     PISSN: 03661644     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (18)

1. Ackers, G. K., Doyle, M. L., and Daugherty, M. A. (1992). Molecular code for cooperativity in hemoglobin. Science 54-63.
2. Sleitz, T. A. (1990). Structural studies of protein-nucleic acid-interactions: the source of sequence-specific binding. Quat. Rev. Biophys. 23: 205-280.
3. Jurnak, F. E: and McPherson, A. Eds. (1984). Biological Macromolecules and Assemblies, Vol. 1. Virus Structure, Wiley.
4. Raghavendra, K., Kelly. JA, Khaillarah, L, and Schuster, T. M. (1988). Structure and function of disk aggregates of the coat protein of tobacco mosaic virus. Biochemistry, 27 : 7583-75888.
5. Maruzza, R. A., Phillips, S. E. V., and Poljak, R. J. (1987). The Structural basis of antigen-antibody recognition. Annu. Rev. Biophys. Biophys. Chem. 16 :139-159.
6. Pelletier, H., and Kraut, J. (1992). Crystal Structure of a complex between electron transfer partners; cytochrome c oxidase and cytochrome c. Science 258 :1448-1755.
7. Privalov, P. L., and Gill, S. J. (1988). Stability of protein structures and hydrophobic interactions. Adv. Prot. Chem. 39 :193-234
8. Glauser, M., Bryant, D. A. . Frank, G., Wehrli, E., Rusconi, S. S., Sidler, W. and Zuber; H. (1992). Phycobilisome structure in the cyanobacteria M. laminosus and Anabaena sp, . PCC7120. Eur. J. Biochem 205(3):907-915
9. Glazer, A. N. (1989). Light guides. J. Biol. Chem. 264(1): 1-4
10. Bunster, M., Tellez, J. and Candia, A. (1997). Characterization of phycobiliproteins present in Gracilaria chilensis. Bol. Soc. Chil. Qufm. 42 : 449-455
11. Contreras-Martel, C., Martinez-Oyanedel, J., Bunster, M., Legrand, P., Piras, C., Venerde, X., and Fontecilia-Camps, J. (2000). Crystallization and 2. 2 A resolution structure of R-phycoerythrin from Gracilaria chilensis: a case of perfect hemihedral twinning. In preparation.
12. Koradi, R., Billeter, M. and Wuthrich, K. (1996). MOLMOL : a program for display and analysis of macromolecular structures. J. Mol. Graphics 14 : 51-54
13. Bunster, M., Bruna, C., Contreras-Martel, C., and Martînez-Oyanedel, J. (2000). Functional Structural analysis of the oligomerization states of R-phycoerythrin from Gracilaria chilensis. Sent to Biophysical Journal.
14. Swanson, R. V., and Glazer, A. N. (1990). Separation of phycobiliprotein subunits by reverse-phase high pressure liquid chromatography. Anal. Biochem. 188(2): 295-299.
15. Schellman, J. A. (1997). Temperature, stability and the hydrophobic interaction. Biophys. J. 73: 2960-2964.
16. Qin Zou, Hubermann-Rottinghaus, S. M., Murphy, K. P. (1998). Urea effect on protein stability: hydrogen bonding and the hydrophobic effect. Proteins: Structure, Function and Genetics. 31 :107-115.
17. Chang, W. R., Jiang, T., Wang, Z. L, Yang, Z. X. and Liang, D. C. (1996). Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2. 8 A resolution. J. Mol. Biol. 262 :721 -731
18. Fluglistaller, P., Suter, F., and Zuber, H. (1986). Linker polypeptides from the cyanobacterium Mastigoclaudus laminosus. II. Aminoacid sequences and function. Biol. Chem. Hoppe Seyler. 367(7): 615-626.