Native fluorescence and Mag-indo-1 -protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin subdomain in the presence of guanidine hydrochloride

Published

Journal Article

Changes in the fluorescence spectrum of tryptophans Trp 134 and Trp 212 in bovine serum albumin (BSA) and of Trp 214 of human serum albumin in the presence of the chaotropic agent guanidine hydrochloride (Gnd) were studied. A detailed analysis of the fluorescence spectrum of native BSA yielded the fluorescence spectrum for each tryptophan of BSA. Modifications in the binding of Mag-indo-1 to BSA, which results in a specific quenching of the fluorescence spectrum of Trp 134 associated with an energy transfer from Trp 134 to the protein-bound Mag-indo-1, were also investigated. Changes occurring when the Gnd concentration is decreased stepwise cover a larger concentration scale of Gnd than the reverse protocol, allowing one to suggest that the resulting conformational changes in the subdomain IA of BSA involve at least three different steps. © 2000 Plenum Publishing Corporation.

Duke Authors

Cited Authors

  • Viallet, PM; Vo-Dinh, T; Ribou, AC; Vigo, J; Salmon, JM

Published Date

  • December 1, 2000

Published In

Volume / Issue

  • 19 / 6

Start / End Page

  • 431 - 439

Electronic International Standard Serial Number (EISSN)

  • 1573-4943

International Standard Serial Number (ISSN)

  • 1572-3887

Citation Source

  • Scopus