Xem trước tài liệu

Đang tải tài liệu...

Thông tin chi tiết tài liệu

Định dạng: PDF
Số trang: 11 trang
Dung lượng: 268 KB

Giới thiệu nội dung

Conformational Changes of β-Lactoglobulin in Sodium Bis(2-ethylhexyl) Sulfosuccinate Reverse Micelles

Authors:

Suzana M. Andrade, Teresa I. Carvalho, M. Isabel Viseu, and Sílvia M. B. Costa

Field:

Biochemistry, Biophysics

Document Content:

This document presents a study on the conformational changes of β-lactoglobulin (BLG) when encapsulated in sodium bis(2-ethylhexyl) sulfosuccinate (AOT) reverse micelles (RM). The research utilizes fluorescence and circular dichroism (CD) spectroscopy to investigate how varying water content (ω₀) within the RM affects the protein’s structure and the environment of its tryptophan (Trp) residues. The findings suggest significant alterations in BLG’s tertiary structure and a distortion of its β-sheet conformation as the water content increases. The study also explores the accessibility of Trp residues to quenchers like acrylamide and CCl₄ to further understand these structural modifications and the protein’s location within the micellar system.

Detailed Table of Contents:

  • Introduction
  • Materials and Methods
  • Results
    • CD spectra of BLG in AOT RM
    • Fluorescence of BLG in AOT RM
    • Fluorescence quenching of Trp residues in BLG
  • Discussion
    • CD data
    • Fluorescence data
    • BLG location on AOT RM
    • Encapsulation effect on the Trp environment
  • Conclusions
  • Acknowledgements
  • References