Por favor, use este identificador para citar o enlazar este ítem: http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2937
Título : Unraveling the mechanisms of tryptophan fluorescence quenching in the triosephosphate isomerase from Giardia lamblia
Creador: Hernández Alcántara, Gloria
Nivel de acceso: Open access
Palabras clave : Giardia lamblia - enzimología
Triosa-Fosfato Isomerasa - química
Triptófano - metabolismo
Giardia lamblia - enzymology
Triose-Phosphate Isomerase - chemistry
Tryptophan - metabolism
Giardia
Triosephosphate isomerase
Glicólisis
Interacción aromática
Espectroscopia
Enfriamiento
Ambiente de triptófano
Giardia
Triosephosphate isomerase
Glycolysis
Aromatic interaction
Spectroscopy
Quenching
Tryptophan environment
Descripción : In the native state several proteins exhibit a quenching of fluorescence of their tryptophans. We studied triosephosphate isomerase from Giardia lamblia (GlTIM) to dissect the mechanisms that account for the quenching of fluorescence of its Trp. GlTIM contains four Trp per monomer (Trp75, Trp162, Trp173, and Trp196) distributed throughout the 3D structure. The fluorescence of the denatured enzyme is 3-fold higher than that of native GlTIM. To ascertain the origin of this phenomenon, single and triple mutants of Trp per Phe were made. The intrinsic fluorescence was determined, and the data were interpreted on the basis of the crystal structure of the enzyme. Our data show that the fluorescence of all Trp residues is quenched through two different mechanisms. In one, fluorescence is quenched by aromatic-aromatic interactions due to the proximity and orientation of the indole groups of Trp196 and Trp162. The magnitude of the quenching of fluorescence in Trp162 is higher than in the other three Trp. Fluorescence quenching is also due to energy transfer to the charged residues that surround Trp 75, 173 and 196. Further analysis of the fluorescence of GlTIM showed that, among TIMs from other parasites, Trp at position 12 exhibits rather unique properties. © 2008.
Colaborador(es) u otros Autores: Rodríguez-Romero A
 Reyes-Vivas H
 Peon J
 Cabrera N
 Ortiz C
 Enríquez-Flores S
 De la Mora-De la Mora I
 López-Velázquez G
Fecha de publicación : 2008
Tipo de publicación: Artículo
Formato: pdf
Identificador del Recurso : 10.1016/j.bbapap.2008.05.016
Fuente: Biochimica et Biophysica Acta - Proteins and Proteomics 1784(11):1493 - 1500
URI : http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2937
Idioma: eng
Aparece en las colecciones: Artículos

Ficheros en este ítem:
No hay ficheros asociados a este ítem.


Los ítems de DSpace están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.