2026-09-22T11:06:44Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/84225 2023-07-11 col_2142_5131 col_2142_14789 com_2142_5130 com_2142_14788 com_2142_8903

Raven Huang Lin, Yi-Lun 2015-09-25T22:13:33Z 2015-09-25T22:13:33Z 10000-01-01 2006 2006 The 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. Made available in DSpace on 2015-09-25T22:13:33Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3223658.pdf: 3100933 bytes, checksum: ded05d527b262dd3454cb5e3b214946a (MD5) Previous issue date: 2006 Embargo set by: Seth Robbins for item 85506 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 121 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2006. http://hdl.handle.net/2142/84225 (MiAaPQ)AAI3223658 eng Biology, Molecular Structure and Function of Colicin E5 Ribonuclease Domain text Chemistry Chemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.