Biography:Marta Bunster

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Short description: Chilean biologist
Marta Bunster
NationalityChile an
Alma materUniversity of Concepción, University of Chile, University of Florida
Known forHydrophobicity profiles method
Scientific career
FieldsBiochemistry, biophysics, crystallography
InstitutionsUniversity of Concepción
Thesis (1981)

Marta Cecilia del Carmen Bunster Balocchi is a Chile an scientist, most noted for her work in the fields of biochemistry, biophysics and crystallography. She is also known as one of the main promoters of bioinformatics in her country.

Biography

She began studying biochemistry in 1969 at the University of Concepción, where she spent most of her academic and professional career.[1] She obtained a biochemistry diploma in 1974 for her work about X-ray diffraction on synthetic polypeptides.[2] After obtaining her degree, she moved to Santiago, where she worked at the laboratory of Osvaldo Cori and Aida Traverso, from the Faculty of Chemical Sciences of the University of Chile. There, she collaborated in the investigation of the kinetic properties of a potato apyrase. After 4 months, she returned to Concepción and entered to the Doctor of Sciences Program, with a major in chemistry. In 1975,[3] she was conferred an academic position as instructor of biophysics for biochemistry teachers at the Department of Phisiology of the Institute of Medical Biological Sciences,[1] precursor of the current Biological Sciences Faculty of the University of Concepción. Bunster obtained her doctoral degree in 1981 for her study on synthetic polymers of pharmacological application, at the University of Concepción and the laboratory of George B. Butler at the University of Florida.[1][3] That year, she returned to Concepción once more and met doctor Hilda Cid, a renowned scientist in the fields of physics and crystallography, who had returned from Sweden after being politically persecuted.[4] During those years, Cid specialized in crystallographic techniques at Uppsala University, which provided her the necessary equipment for her studies once she returned to Chile.[4][5][6] Together, they established the Molecular Biophysics Laboratory of the Faculty of Biological Sciences and Natural Resources, now the Faculty of Biological Sciences,[6][7] and started studying new methods for proteins structures and folding prediction. Among their first research was the development of the secondary structures prediction method by means of hydrophobicity profiles,[8] which was greatly welcomed in the region due to its high reliability and low cost,[9][10][11][12] being one of the bases of some of the modern techniques.[13][14][15] In the mid 90's, and coinciding with Cid's retirement, Bunster investigated phycobilisomes,[16] a fluorescent, macromolecular-light harvesting system present primarily in cyanobacteria and red algae. This research led to the development of spectroscopic techniques[17][18] and its application.[19][20] It allowed a greater understanding of conformational changes phenomena from a physical perspective.[21]

Legacy

In the 2000s, driven by the boom of bioinformatics, Bunster dedicated her efforts to consolidating international cooperation in this area, forming in 2002 the Iberoamerican Network for Bioinformatics, later renamed as Iberoamerican Society for Bioinformatics (SoIBio),[3][22] institution in which she assumed a directive role as Secretary on its first executive board,[23] and on which she remains active to this day.

She was part of the Biological Sciences Doctoral Program since its creation,[3] as well as one of the founding members and Director of the Master in Biochemistry and Bioinformatics and the Director of the Biochemistry and Molecular Biology Department from 2014 until her retirement in 2020.[1][3]

Organizational activity

Bunster has been part of numerous scientific organizations during her career, both in Chile and abroad. Some of them include: Chilean Chemical Society, Chilean Biology Society, Society of Biochemistry and Molecular Biology of Chile, Biophysical Society, International Society for Computational Biology (ISCB), and the Latin American Cristallographic Association (LACA).[3]

Featured publications

  • Cid, H., Bunster, M., Arriagada, E., & Campos, M. (1982). Prediction of secondary structure of proteins by means of hydrophobicity profiles. FEBS Letters, 150(1), 247–254. https://doi.org/10.1016/0014-5793(82)81344-6.
  • Cid, H., Vargas, V., Bunster, M., & Bustos, S. (1986). Secondary structure prediction of human salivary proline-rich proteins. FEBS letters, 198(1), 140–144. https://doi.org/10.1016/0014-5793(86)81200-5.
  • Cid, H., Bunster, M., Canales, M., & Gazitúa, F. (1992). Hydrophobicity and structural classes in proteins. Protein engineering, 5(5), 373–375. https://doi.org/10.1093/protein/5.5.373.
  • Contreras-Martel, C., Martinez-Oyanedel, J., Bunster, M., Legrand, P., Piras, C., Vernede, X., & Fontecilla-Camps, J. C. (2001). Crystallization and 2.2 Å resolution structure of R-phycoerythrin from Gracilaria chilensis: a case of perfect hemihedral twinning. Acta crystallographica. Section D, Biological crystallography, 57(Pt 1), 52–60. https://doi.org/10.1107/s0907444900015274.
  • Godoy, F. A., Bunster, M., Matus, V., Aranda, C., González, B., & Martínez, M. A. (2003). Poly-beta-hydroxyalkanoates consumption during degradation of 2,4,6-trichlorophenol by Sphingopyxis chilensis S37. Letters in applied microbiology, 36(5), 315–320. https://doi.org/10.1046/j.1472-765x.2003.01315.x.
  • Martínez-Oyanedel, J., Contreras-Martel, C., Bruna, C., & Bunster, M. (2004). Structural-functional analysis of the oligomeric protein R-phycoerythrin. Biological Research, 37(4). https://doi.org/10.4067/s0716-97602004000500003.
  • Tobella, L. M., Bunster, M., Pooley, A., Becerra, J., Godoy, F., & Martínez, M. A. (2005). Biosynthesis of poly-beta-hydroxyalkanoates by Sphingopyxis chilensis S37 and Wautersia sp. PZK cultured in cellulose pulp mill effluents containing 2,4,6-trichlorophenol. Journal of industrial microbiology & biotechnology, 32(9), 397–401. https://doi.org/10.1007/s10295-005-0011-1.
  • Contreras-Martel, C., Matamala, A., Bruna, C., Poo-Caamaño, G., Almonacid, D., Figueroa, M., Martínez-Oyanedel, J., & Bunster, M. (2007). The structure at 2 Å resolution of Phycocyanin from Gracilaria chilensis and the energy transfer network in a PC-PC complex. Biophysical chemistry, 125(2-3), 388–396. https://doi.org/10.1016/j.bpc.2006.09.014.
  • Figueroa, M., Hinrichs, M. V., Bunster, M., Babbitt, P., Martinez-Oyanedel, J., & Olate, J. (2009). Biophysical studies support a predicted superhelical structure with armadillo repeats for Ric-8. Protein science, 18(6), 1139–1145. https://doi.org/10.1002/pro.124.
  • Burgos, C. F., Castro, P. A., Mariqueo, T., Bunster, M., Guzmán, L., & Aguayo, L. G. (2015). Evidence for α-helices in the large intracellular domain mediating modulation of the α1-glycine receptor by ethanol and Gβγ. The Journal of pharmacology and experimental therapeutics, 352(1), 148–155. https://doi.org/10.1124/jpet.114.217976.
  • Sivakumar, R., Manivel, A., Meléndrez, M., Martínez-Oyanedel, J., Bunster, M., Vergara, C., & Manidurai, P. (2015). Novel heteroleptic ruthenium sensitizers containing carbazole linked 4,5-diazafluorene ligand for dye sensitized solar cells. Polyhedron, 87, 135–140. https://doi.org/10.1016/j.poly.2014.11.008.
  • Vásquez-Suárez, A., Lobos-González, F., Cronshaw, A., Sepúlveda-Ugarte, J., Figueroa, M., Dagnino-Leone, J., Bunster, M., & Martínez-Oyanedel, J. (2018). The γ33 subunit of R-phycoerythrin from Gracilaria chilensis has a typical double linked phycourobilin similar to β subunit. PLOS ONE, 13(4), e0195656. https://doi.org/10.1371/journal.pone.0195656.

References

  1. ↑ 1.0 1.1 1.2 1.3 "PDI - Resultado de Búsqueda". https://investigadores.anid.cl/es/public_search/researcher?id=3060. 
  2. ↑ Suwalsky, M.; Bunster, M.; Wagner, K. G. (1975). "An X-ray diffraction study of poly-L-homoarginine hydrochloride" (in en). Biopolymers 14 (6): 1197–1204. doi:10.1002/bip.1975.360140608. ISSN 1097-0282. PMID 1164543. https://onlinelibrary.wiley.com/doi/abs/10.1002/bip.1975.360140608. 
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 "Marta Bunster (talk Osvaldo Cori), exhibiting confirmed XLI annual meeting of the society of Biochemistry and Molecular Biology of Chile, 25 to 28 of September 2018, Iquique, Chile | Society for Biochemistry and Molecular Biology of Chile" (in en). https://www.sbbmch.cl/?p=15326&lang=en. 
  4. ↑ 4.0 4.1 "Hilda Cid: La primera chilena en doctorarse en Ciencias Exactas y cuyos logros han caído en el olvido | Sociedad de Bioquímica y Biología Molecular de Chile" (in en). https://www.sbbmch.cl/?p=4852&lang=en. 
  5. ↑ "- CRECES". http://www.creces.cl/Contenido?art=2. 
  6. ↑ 6.0 6.1 "Hilda Cid, una pionera chilena en cristalografía | Vidas científicas" (in es). 2020-10-13. https://mujeresconciencia.com/2020/10/13/hilda-cid-una-pionera-chilena-en-cristalografia/. 
  7. ↑ "Historia" (in es). https://cienciasbiologicasudec.cl/historia/. 
  8. ↑ Cid, Hilda; Bunster, Marta; Arriagada, Eugenio; Campos, María (1982). "Prediction of secondary structure of proteins by means of hydrophobicity profiles" (in en). FEBS Letters 150 (1): 247–254. doi:10.1016/0014-5793(82)81344-6. ISSN 1873-3468. https://onlinelibrary.wiley.com/doi/abs/10.1016/0014-5793%2882%2981344-6. 
  9. ↑ Valle, Fernando; Becerril, Baltazar; Chen, Ellson; Seeburg, Peter; Heyneker, Herbert; Bolivar, Francisco (1984-02-01). "Complete nucleotide sequence of the glutamate dehydrogenase gene from Escherichia coli K-12" (in en). Gene 27 (2): 193–199. doi:10.1016/0378-1119(84)90140-9. ISSN 0378-1119. PMID 6373501. https://dx.doi.org/10.1016/0378-1119%2884%2990140-9. 
  10. ↑ Beltran, J. R.; Mascarenhas, Y. P.; Craievich, A. F.; Laure, C. J. (1990-01-01). "SAXS study of the snake toxin α-crotamine" (in en). European Biophysics Journal 17 (6): 325–329. doi:10.1007/BF00258381. ISSN 1432-1017. PMID 2307140. https://doi.org/10.1007/BF00258381. 
  11. ↑ Ponnuswamy, P. K. (1993-01-01). "Hydrophobic characteristics of folded proteins" (in en). Progress in Biophysics and Molecular Biology 59 (1): 57–103. doi:10.1016/0079-6107(93)90007-7. ISSN 0079-6107. PMID 8419986. 
  12. ↑ Klein, Petr; Delisi, Charles (1986). "Prediction of protein structural class from the amino acid sequence" (in en). Biopolymers 25 (9): 1659–1672. doi:10.1002/bip.360250909. ISSN 1097-0282. PMID 3768479. https://onlinelibrary.wiley.com/doi/abs/10.1002/bip.360250909. 
  13. ↑ Shu, Jian-Jun; Yong, Kian Yan (2017-04-15). "Fourier-based classification of protein secondary structures" (in en). Biochemical and Biophysical Research Communications 485 (4): 731–735. doi:10.1016/j.bbrc.2017.02.117. ISSN 0006-291X. PMID 28246013. https://www.sciencedirect.com/science/article/pii/S0006291X17304084. 
  14. ↑ Perunov, Nikolay; England, Jeremy L. (2014). "Quantitative theory of hydrophobic effect as a driving force of protein structure" (in en). Protein Science 23 (4): 387–399. doi:10.1002/pro.2420. ISSN 1469-896X. PMID 24408023. 
  15. ↑ Wang, Han; He, Zhiquan; Zhang, Chao; Zhang, Li; Xu, Dong (2013-07-19). "Transmembrane Protein Alignment and Fold Recognition Based on Predicted Topology" (in en). PLOS ONE 8 (7): e69744. doi:10.1371/journal.pone.0069744. ISSN 1932-6203. PMID 23894534. 
  16. ↑ "Characterization of phycobiliproteins present in Gracilaria chilensis". Boletin de la Sociedad Chilena de Quimica 42: 449–455. https://www.researchgate.net/publication/328285811. 
  17. ↑ Contreras-Martel, C.; Martinez-Oyanedel, J.; Bunster, M.; Legrand, P.; Piras, C.; Vernede, X.; Fontecilla-Camps, J.-C. (2001-01-01). "Crystallization and 2.2 Å resolution structure of R-phycoerythrin from Gracilaria chilensis: a case of perfect hemihedral twinning" (in en). Acta Crystallographica Section D: Biological Crystallography 57 (1): 52–60. doi:10.1107/S0907444900015274. ISSN 0907-4449. PMID 11134927. http://scripts.iucr.org/cgi-bin/paper?ol0021. 
  18. ↑ Matamala, Adelio R.; Almonacid, Daniel E.; Figueroa, Maximiliano F.; Martínez-Oyanedel, José; Bunster, Marta C. (May 2007). "A semiempirical approach to the intra-phycocyanin and inter-phycocyanin fluorescence resonance energy-transfer pathways in phycobilisomes". Journal of Computational Chemistry 28 (7): 1200–1207. doi:10.1002/jcc.20628. ISSN 0192-8651. PMID 17299727. https://pubmed.ncbi.nlm.nih.gov/17299727/. 
  19. ↑ Saavedra, R.; Figueroa, M.; Wandersleben, T.; Pouchucq, L.; Morales, J. E.; Bunster, M.; Cruz-Orea, A. (June 2005). "In situ photoacoustic spectroscopy of phycobiliproteins in Gracilaria chilensis". Journal de Physique IV (Proceedings) 125: 765–767. doi:10.1051/jp4:2005125176. ISSN 1155-4339. http://www.edpsciences.org/10.1051/jp4:2005125176. 
  20. ↑ Sivakumar, Radhakrishnan; Manivel, Arumugam; Meléndrez, Manuel; Martínez-Oyanedel, José; Bunster, Marta; Vergara, Carola; Manidurai, Paulraj (2015-02-17). "Novel heteroleptic ruthenium sensitizers containing carbazole linked 4,5-diazafluorene ligand for dye sensitized solar cells" (in en). Polyhedron 87: 135–140. doi:10.1016/j.poly.2014.11.008. ISSN 0277-5387. https://www.sciencedirect.com/science/article/pii/S0277538714007153. 
  21. ↑ Martínez-Oyanedel, José; Contreras-Martel, Carlos; Bruna, Carola; Bunster, Marta (2004). "Structural-functional analysis of the oligomeric protein R-phycoerythrin". Biological Research 37 (4): 733–745. doi:10.4067/S0716-97602004000500003. ISSN 0716-9760. PMID 15586822. http://www.scielo.cl/scielo.php?script=sci_abstract&pid=S0716-97602004000500003&lng=en&nrm=iso&tlng=en. 
  22. ↑ "History of SoIBio | Sociedad Iberoamericana de Bioinformática / Iberoamerican Society for Bioinformatics (SoIBio)". https://www.soibio.org/en/history. 
  23. ↑ "Founder Members (Mexico, October 2009) | Sociedad Iberoamericana de Bioinformática / Iberoamerican Society for Bioinformatics (SoIBio)". https://www.soibio.org/en/founderMembers. 



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