KOPRI Repository

Characterization and preliminary X-ray crystallographic analysis of an Ice-binding protein (FfIBP) from phychrophilic bacteria, Flavobacterium frigoris

Metadata Downloads
Title
Characterization and preliminary X-ray crystallographic analysis of an Ice-binding protein (FfIBP) from phychrophilic bacteria, Flavobacterium frigoris
Other Titles
호냉성 박테리아 (Flavobacterium frigoris)종이 분비하는 결빙방지단백질의 구조적 기초조사 및 특징
Authors
Do, Hackwon
Lee, Sung Gu
Kim, Hak Jun
Lee, Jun Hyuck
Issue Date
2012
Citation
Do, Hackwon, et al. 2012. Characterization and preliminary X-ray crystallographic analysis of an Ice-binding protein (FfIBP) from phychrophilic bacteria, Flavobacterium frigoris. 한국생물공학회. 한국생물공학회. 2012.04.11~.
Abstract
The Ice binding protein (IBP) is a prerequisite material for organism to be allowed to live in a subzero environment. Ice growth in a cold environment is fatal for organism which is not just physically destruction of inner cell organelle but also chemical damage such an osmotic shock. IBP has been characterized property of which ability inhibit the ice growth by binding to specific ice plane. Flavobacterium frigoris isolated from Antarctic area produce an ice-binding protein (FfIBP) to survive and reduce damage from ice growth. The FfIBP has been cloned and over-expressed in Escherichia coli. To diagnose ice-binding mechanism, we measured thermal hysteresis (TH) activity which is numerical value of a gap between freezing and melting point as well as ice re-crystallization inhibition activity. Thermal hysteresis activity of the FfIBP was approximately 2.5℃ at 50uM that is 10 times higher than moderately active LeIBP. Furthermore, the Ice Re-crystallization inhibition activity represent the FfIBP has ability to inhibit ice growing at low concentration 2.5uM limit. Consequently the FfIBP was classified as a hyper-active Ice binding protein. Also, preliminary X-ray crystallography was performed to reveal the ice-binding site of FfIBP at the molecular level.e but also chemical damage such an osmotic shock. IBP has been characterized property of which ability inhibit the ice growth by binding to specific ice plane. Flavobacterium frigoris isolated from Antarctic area produce an ice-binding protein (FfIBP) to survive and reduce damage from ice growth. The FfIBP has been cloned and over-expressed in Escherichia coli. To diagnose ice-binding mechanism, we measured thermal hysteresis (TH) activity which is numerical value of a gap between freezing and melting point as well as ice re-crystallization inhibition activity. Thermal hysteresis activity of the FfIBP was approximately 2.5℃ at 50uM that is 10 times higher than moderately a
URI
http://repository.kopri.re.kr/handle/201206/8442
Conference Name
한국생물공학회
Conference Place
한국생물공학회
Conference Date
2012.04.11~
Files in This Item
General Conditions
      ROMEO Green
    Can archive pre-print and post-print or publisher's version/PDF
      ROMEO Blue
    Can archive post-print (ie final draft post-refereeing) or publisher's version/PDF
      ROMEO Yellow
    Can archive pre-print (ie pre-refereeing)
      ROMEO White
    Archiving not formally supported

    qrcode

    Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

    Browse