Probing the Structure of Apolipoprotein AI by Specific Fluorescent Labeling of Introduced Cysteine Residues
Behling-Agree, Andrea Kristin
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Permalink
https://hdl.handle.net/2142/84917
Description
Title
Probing the Structure of Apolipoprotein AI by Specific Fluorescent Labeling of Introduced Cysteine Residues
Author(s)
Behling-Agree, Andrea Kristin
Issue Date
2000
Doctoral Committee Chair(s)
Jonas, Ana
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biophysics, General
Language
eng
Abstract
Based on this study and previous results, a model of lipid-free proapoAI was constructed. This model takes into account the elongated shape of proapoAI, indicates that the N- and C-terminal extremes of proapoAI are compact, the C-terminal region is within 40 A of the 5 Trp residues in the N-terminal half of the sequence, and that the 5th helix is most distant from the N-terminal half of proapoAI.
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