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  E-mail Message: I thought you might be interested in this item at http://www.worldcat.org/oclc/952152617 Title: Expression chez E. coli de protéines impliquées dans le cancer ainsi que le SIDA, et études par RMN du solide de molécules antibactériennes Author: Marc Prudhon; Burkhard Bechinger; Université de Strasbourg (2009-....); École doctorale Sciences chimiques (Strasbourg / 1995-....) Publisher: 2011. OCLC:952152617

  
  

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Expression chez E. coli de protéines impliquées dans le cancer ainsi que le SIDA, et études par RMN du solide de molécules antibactériennes

Author:	Marc Prudhon; Burkhard Bechinger; Université de Strasbourg (2009-....).; École doctorale Sciences chimiques (Strasbourg / 1995-....).
Publisher:	2011.
Dissertation:	Thèse de doctorat : Chimie : Strasbourg : 2011.
Edition/Format:	Thesis/dissertation : Thesis/dissertation : Manuscript  Archival Material : French
Summary:	Membrane proteins represent 30% of human genome coding sequences. Study of the membrane proteins is limited by the difficulty to produce big quantities to perform measurement in membrane environment. We have worked on different membrane proteins during this thesis. Firstly, we have studied NK-2 peptide. This antimicrobial charged and amphipathic 27 amino acids peptide has been produced labeled with 15N in two different positions. Interaction of the peptide with oriented POPG membrane and deuterated POPC/POPGd31 vesicles has been measured by ssNMR. Our results show the peptide oriented parallel to the membrane and inserted in the lipids at about 6Å depth. We have so brought out a carpet type action model. We have also designed amino acids sequences named gp41-TM, gp120-TM and FP-TM. These proteins can expose sequences of the envelop proteins from HIV linked to a peptide TM, with the goal to produce a potential vaccine against AIDS. We have demonstrated that TM peptide takes an alpha helix structure, it oriented perpendicular to the membrane (transmembrane) and is able to form trimmers in micelles. We have developed an over expression system of these three proteins with E. coli. Expression vectors coding for the proteins have been constructed using pTPIX4 in fusion with TAF12 protein. The proteins expressed in membrane fraction, so we have established purification protocol using delipidation of the membrane fraction before using HPLC. Finally, we have tested E. coli expression and purification of the Bax protein in fusion with MBP, to obtain an effective method of production of this pro apoptotic protein. We have demonstrated that this system is not enough sufficient.  Read more...