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|Type:||Artigo de periódico|
|Title:||Effects of trifluoperazine on the conformation and dynamics of membrane proteins in human erythrocytes|
|Abstract:||The chemical modifications induced by trifluoperazine (TFP) in erythrocyte ghosts have been investigated by fluorescence quenching. The apparent distance separating the membrane protein tryptophans and bound 1-aniline-8-naphthalene sulfonate (ANS) molecules decreased after treating erythrocyte membranes with TFP. This effect was accompanied by a significant decrease in the maximum efficiency of energy transfer. We conclude that TFP-induced alterations in the structure of membrane proteins lead to a rearrangement of the surrounding lipids, and consequently to local conformational changes in membrane organization. (C) 1998 Academic Press.|
|Editor:||Academic Press Inc|
|Citation:||Molecular Genetics And Metabolism. Academic Press Inc, v. 64, n. 2, n. 148, n. 151, 1998.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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