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Study of the pH‐Dependent Conformational Changes in α1‐Acid Glycoprotein Using FRET
Author(s) -
MIKHAILOV ALEXEI S.
Publication year - 2005
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1342.064
Subject(s) - chemistry , förster resonance energy transfer , biophysics , glycoprotein , conformational change , single molecule fret , biochemistry , fluorescence , biology , physics , quantum mechanics
A bstract : We studied pH‐dependent conformational changes in α1‐acid glycoprotein using both binding of cationic fluorescent probe Quinaldine Red with protein molecule and changes in distance between tryptophan from binding site of the protein and Calcofluor White on glycan surface using FRET. Our data show that the binding site of the protein has undergone a conformational change at pH 9.0. At this pH. the binding site forms a more hydrophobic region and tryptophan residues from the binding site move to the center of the protein core.