Acceso a usuarios
Bienvenid@

Tutores

MIGUEL ANTONIO COSTAS BASIN

Facultad de Química (FQ)

Contacto

Teléfono: 55 56223169
Email: costasmi@unam.mx
Sitio web: Visitar sitio web

Campos de conocimiento

Biofísica
Bioquímica
Reconocimiento Molecular y Bioestructura

Líneas de investigación

Bio-fisicoquímica. Bases energetico estructurales de la estabilidad cinetica y termodinamica de las proteinas

Publicaciones

115. Localized conformational changes trigger the pH-induced fibrillogenesis of
an amyloidogenic λ light chain protein
Isabel Velázquez-López, Gilberto Valdés-García, Sergio Romero Romero, Roberto Maya Martínez, Ana I. Leal-Cervantes, Miguel Costas, Rosana Sánchez-López, Carlos Amero, Nina Pastor, D. Alejandro Fernández Velasco.
Biochim. Biophys. Acta - General Subjects, 2018, 1862, 1656-1666. htpps://doi.org/10.1016/j.bbagen.2018.04.014

114. Complexation Thermodynamics of α-Cyclodextrin with Ionic Surfactants in Water.
Daniel Ondo, Miguel Costas
J. Colloid and Interface Science, 2017, 505, 445-453.
DOI: dx.doi.org/10.1016/j.jcis.2017.05.093

113. A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability and human disease.
Vanesa Olivares-Illana, Hector Riveros-Rosas, Nallely Cabrera, Marietta Tuena de Gómez-Puyou, Ruy Pérez-Montfort, Miguel Costas, Armando Gómez-Puyou
PROTEINS: Structure, Function, and Bioinformatics, 2017, 85, 1190-1211.
DOI: 10.1002/prot.25299

112. The effect of specific proline residues on the kinetic stability of the triosephosphate isomerases of two trypanosomes.
Valeria Guzmán-Luna, Andrea G. Quezada, A. Jessica Díaz-Salazar, Nallely Cabrera, Ruy Pérez-Montfort, Miguel Costas
PROTEINS: Structure, Function, and Bioinformatics, 2017, 85, 571-579
DOI: 10.1002/prot.25231

111. Interplay between Protein Thermal Flexibility and Kinetic Stability
Andrea G. Quezada, A. Jessica Díaz-Salazar, Nallely Cabrera, Ruy Pérez-Montfort, Ángel Piñeiro, Miguel Costas
Structure, 2017, 25, 167-179.
http://dx.doi.org/10.1016/j.str.2016.11.018

110. Stability and aggregation propensity do not fully account for the association of various germline variable domain gene segments with light chain amyloidosis.
Sergio Garay-Sánchez, Francisco Rodriguez-Alvarez, Guadalupe Zavala-Padilla, Luz Mejia-Cristobal, Armando Cruz-Rangel, Miguel Costas, D. Alejandro Fernández-Velasco, Jorge Meléndez-Zajgla, Luis del Pozo-Yauner.
Biological Chemistry, 2017, 398(4), 477-489.
DOI: https://doi.org/10.1515/hsz-2016-0178

109. Protein-protein interactions at high concentrations. Isothermal titration calorimetry determination of human serum albumin-lysozyme interaction enthalpy at several pH values.
María Teresa Vieyra-Eusebio, Miguel Costas
Thermochimica Acta, 2016, 641, 39-42. doi: 10.1016/j.tca.2016.08.011



108. Complex Behavior of Aqueous α-Cyclodextrin Solutions. Interfacial Morphologies Resulting from Bulk Aggregation.
Jorge Hernandez-Pascacio, Ángel Piñeiro, Juan M. Ruso, Natalia Hassan, Richard A. Campbell, José Campos-Terán, Miguel Costas
Langmuir, 2016, 32,6682-6690. doi:10.1021/acs.langmuir.6b01646,

107. Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains.
C. Aguirre, Y. Goto, M. Costas
FEBS Letters, 2016, 590, 202-214. doi:10.1002/1873-3468.12041

106. Size product modulation by enzyme concentration reveals two distinct levan elongation mechanisms in Bacillus subtilis levansucrase.
Enrique Raga-Carbajal, Ernesto Carrillo-Nava, Miguel Costas, Jaime Porras-Dominguez, Agustin Lopez-Munguia , Clarita Olvera
Glycobiology, 2016, 26 (4), 377-385. doi: 10.1093/glycob/cwv112

105. Intrinsic levanase activity of Bacillus subtilis 168 levansucrase (SacB).
Luz Méndez-Lorenzo, Jaime R. Porras-Domínguez, Enrique Raga-Carbajal, Clarita Olvera, Maria Rodríguez-Alegría, Ernesto Carrillo-Nava, Miguel Costas, Agustín López-Munguía
PLoS ONE, 2015, 10(11): e0143394, doi:10.1371/journal.pone.0143394

104. Reversibility and two state behaviour in the thermal unfolding of oligomeric TIM barrelproteins.
Sergio Romero-Romero, Miguel Costas, Adela Rodríguez-Romero, D. Alejandro Fernández-Velasco
Phys. Chem. Chem. Phys., 2015, 17, 20699-20714. doi:10.1039/c5cp01599e

103. Isothermal titration calorimetry determination of individual rate constants of trypsin catalytic activity.
C. Aguirre, I. Condado-Morales, L. F. Olguin, M. Costas
Anal. Biochem., 2015, 479, 18-27. doi:10.1016/j.ab.2015.03.014

102. Different contribution of conserved amino acids to the global properties of Triosephosphate isomerases
Y. Aguirre, N. Cabrera, B. Aguirre, R. Pérez-Montfort, A. Hernandez-Santoyo, H. Reyes-Vivas, S. Enríquez-Flores, M. Tuena de Gómez-Puyou, A.Gómez-Puyou, J. M. Sanchez-Ruiz, M. Costas
PROTEINS: Structure, Function, and Bioinformatics, 2014, 82, 323-335. doi: 10.1002/prot.24398


101. The influence of non polar and polar molecules in mouse motile cells membranes and pure lipid bilayers
F. J. Sierra-Valdez, L. S. Forero-Quintero, P. A. Zapata-Morin, M. Costas, A. Chavez-Reyes, J. C. Ruiz-Suarez
PLoS ONE, 2013, 8(4): e59364. doi:10.1371/journal.pone.0059364
Circuito de Posgrado, Ciudad Universitaria
Alcaldía Coyoacán, C.P. 04510, México, CDMX

55 5623 7006
mdcbq@posgrado.unam.mx
UNAM Posgrado