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Studies of Disulfide Bridge Formation in Human Carbonic Anhydrase Between Engineered Cysteines in Non Ideal Conformations Under Equilibrium and Kinetic Conditions
Linköping University, The Department of Physics, Chemistry and Biology.
2007 (English)Independent thesis Advanced level (degree of Magister), 20 points / 30 hpStudent thesisAlternative title
Studier av disulfidbryggebildning i humant karboanhydras mellan genom mutagenes införda cysteiner i icke-ideala konformationer vid jämvikts och kinetiska förhållanden (Swedish)
Abstract [en]

Stabilization of proteins is of great interest for the biotechnological society, industrial as well as research areas. Proteins with high stability are more suitable as reagents, easier to handle, store, transport and use in industrial processes. One way to stabilize a protein is to introduce a disulfide bridge into the structure by protein engineering. In this report the formation of a disulfide bridge between engineered cysteines in non ideal conformations in human carbonic anhydrase has been investigated. The disulfide bridge is not formed when the protein is in its native state. It is shown that when the protein is exposed to mild concentrations of urea in the presence of DTTox the disulfide bridge is formed. Also upon refolding in vitro, in a non oxidative environment, disulfide bridges are formed. This observation is worth to notice, since the disulfide bridge does not form to any appreciable extent when the protein is expressed and folded in vivo in Escherichia coli.

Place, publisher, year, edition, pages
Institutionen för fysik, kemi och biologi , 2007. , 36 p.
Keyword [en]
Disulfide bridge, cysteines, non ideal conformation, equilibrium conditions, kinetic conditions
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:liu:diva-9120ISRN: LITH-IFM-EX--06/1667--SEOAI: oai:DiVA.org:liu-9120DiVA: diva2:23758
Uppsok
fysik/kemi/matematik
Supervisors
Examiners
Available from: 2007-06-07 Created: 2007-06-07

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CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf