From: jbardwel@UMICH.EDU
Subject: Protein folding and disulfide bond formation in E. coli
To: SJD-CHEMISTRY@LISTSERV.UNI-HEIDELBERG.DE
Received: Wednesday, 10 November, 2010, 4:56 PM
SCIENCE-JOBS-DE Stellenausschreibung (vacancies)
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Dieses Angebot wurde eingegeben bei http://www.drarbeit.de,
der Internet-Stellenboerse und Kooperationspartner von
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Fachgebiete: Biologie Chemie Physik
Thema: Doktorarbeit / Diplomarbeit: Protein folding and disulfide bond formation in E. coli
Ansprechpartner: Prof. James Bardwell
Antwort an: jbardwel@umich.edu
Institution: Molecular, Cellular and Developmental Biology
Ort: 44109 Ann Arbor, MI, USA, 830 N University Ave
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One of the fundamental unsolved problems in biology is how proteins attain their proper three dimensional conformations. Heat shock proteins and protein folding catalysts are vital in assisting proteins in this process. Understanding how the protein folding process is assisted is important to understand not just the vital protein folding itself, but also the numerous pathologies, like Alzheimer's, that result from defective protein folding. To determine how protein folding and stability are determined in vivo, we have developed a strong genetic selection that directly links the stability of a protein to an easily selectable marker – antibiotic resistance.
Using directed evolution, we are able to select on the one hand for variants of a target protein that are thermodynamically or kinetically stabilized or, on the other hand, for folding factors that are especially suitable to enhance the expression of recombinant proteins.
Other major projects in the lab are the detailed in vitro characterization of the mechanism of the acid stress chaperone, HdeA, and othes periplasmic chaperones. This involves probing the conformation of the chaperones under various conditions, studying chaperone-substrate interactions, and the fate of substrate proteins following chaperone inactivation.
Furthermore, we are experimentally evolving enzymes that are involved in the disulfide bond formation and isomerization in the model organism E. coli.
Methoden:
We are using a multifaceted genetic, biophysical and structural approach to investigate protein folding, including techniques like cloning, site-directed and random mutagenesis, enzymatic assays, Western blots, spectroscopic techniques (including UV-vis absorbance, fluorescence, FRET and circular dichroism), rapid mixing (stopped flow), protein purification and other.
Anfangsdatum: 11. November 2010
geschätzte Dauer: Diploma/Master: >6 months, PhD: 3 years
Bezahlung: see below
Veröffentlichungen:
http://www.mcdb.lsa.umich.edu/labs/bardwell/publications.php
Homepage: http://www.mcdb.lsa.umich.edu/labs/bardwell/index.php
Internship: at least 3 months, $900/month
Diploma/master thesis: >6 months, $1400/month
PhD thesis: 3 years, $2100/month
Please send a CV, a list of classes taken, recent transcripts and contact information for at least two references to jbardwel@umich.edu.
Subject: Protein folding and disulfide bond formation in E. coli
To: SJD-CHEMISTRY@LISTSERV.UNI-HEIDELBERG.DE
Received: Wednesday, 10 November, 2010, 4:56 PM
SCIENCE-JOBS-DE Stellenausschreibung (vacancies)
----------------------------------------------------------------------
Dieses Angebot wurde eingegeben bei http://www.drarbeit.de,
der Internet-Stellenboerse und Kooperationspartner von
SCIENCE-JOBS-DE für Diplom- und Promotionsarbeiten
----------------------------------------------------------------------
Fachgebiete: Biologie Chemie Physik
Thema: Doktorarbeit / Diplomarbeit: Protein folding and disulfide bond formation in E. coli
Ansprechpartner: Prof. James Bardwell
Antwort an: jbardwel@umich.edu
Institution: Molecular, Cellular and Developmental Biology
Ort: 44109 Ann Arbor, MI, USA, 830 N University Ave
----------------------------------------------------------------------
One of the fundamental unsolved problems in biology is how proteins attain their proper three dimensional conformations. Heat shock proteins and protein folding catalysts are vital in assisting proteins in this process. Understanding how the protein folding process is assisted is important to understand not just the vital protein folding itself, but also the numerous pathologies, like Alzheimer's, that result from defective protein folding. To determine how protein folding and stability are determined in vivo, we have developed a strong genetic selection that directly links the stability of a protein to an easily selectable marker – antibiotic resistance.
Using directed evolution, we are able to select on the one hand for variants of a target protein that are thermodynamically or kinetically stabilized or, on the other hand, for folding factors that are especially suitable to enhance the expression of recombinant proteins.
Other major projects in the lab are the detailed in vitro characterization of the mechanism of the acid stress chaperone, HdeA, and othes periplasmic chaperones. This involves probing the conformation of the chaperones under various conditions, studying chaperone-substrate interactions, and the fate of substrate proteins following chaperone inactivation.
Furthermore, we are experimentally evolving enzymes that are involved in the disulfide bond formation and isomerization in the model organism E. coli.
Methoden:
We are using a multifaceted genetic, biophysical and structural approach to investigate protein folding, including techniques like cloning, site-directed and random mutagenesis, enzymatic assays, Western blots, spectroscopic techniques (including UV-vis absorbance, fluorescence, FRET and circular dichroism), rapid mixing (stopped flow), protein purification and other.
Anfangsdatum: 11. November 2010
geschätzte Dauer: Diploma/Master: >6 months, PhD: 3 years
Bezahlung: see below
Veröffentlichungen:
http://www.mcdb.lsa.umich.edu/labs/bardwell/publications.php
Homepage: http://www.mcdb.lsa.umich.edu/labs/bardwell/index.php
Internship: at least 3 months, $900/month
Diploma/master thesis: >6 months, $1400/month
PhD thesis: 3 years, $2100/month
Please send a CV, a list of classes taken, recent transcripts and contact information for at least two references to jbardwel@umich.edu.
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