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University of Illinois at Urbana-Champaign
Structure and Function of Colicin E5 Ribonuclease Domain
Abstract
dc:descriptionThe binding of ImmE5 to ColE5 resulted in a 50% increase of fluorescence emissions. The isothermal titration calorimetry studies showed a -10 kcal/mol enthalpy change upon the formation of ColE5•ImmE5 complex. The mutational studies of ImmE5 indicated that ImmE5 K4 and D95 contributes a larger inhibitory effect toward ColE5. The structure comparison of ColE5 in homodimer and complex showed that ImmE5 not only blocked but also closed the cleft of the active site of ColE5.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Chemistry
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2015
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Lin, Yi-Lun
- Contributors dc:contributor
-
- Raven Huang
Subjects
dc:subject × 1Rights
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- (MiAaPQ)AAI3223658
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/84225