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University of Illinois at Urbana-Champaign
Probing the Structure of Apolipoprotein AI by Specific Fluorescent Labeling of Introduced Cysteine Residues
Abstract
dc:descriptionBased 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.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Biochemistry
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2015
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Behling-Agree, Andrea Kristin
- Contributors dc:contributor
-
- Jonas, Ana
Subjects
dc:subject × 1Rights
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- (MiAaPQ)AAI9989940
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/84917