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        <title>Biowww.net RSS feed</title>
        <description><![CDATA[BioNews feeds from biowww dot net]]></description>
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        <item>
            <title>Isolation of proteins from inclusion bodies</title>
            <link>http://biowww.net/detail-339.html</link>
            <description>Protocol of isolation of proteins from inclusion bodies is from Bjorkman's group at California Institute of Technology. ...</description>
            <author>biowww</author>
        </item>
        <item>
            <title>E.coli Expression and Renaturing Protocols</title>
            <link>http://biowww.net/detail-342.html</link>
            <description>Protocol from Bjorkman group at CIT. ...</description>
            <author>biowww</author>
        </item>
        <item>
            <title>PREPARATION OF BACTERIALLY EXPRESSED RECOMBINANT GST-FUSION PROTEINS</title>
            <link>http://biowww.net/detail-1033.html</link>
            <description>Protocol by Helen in Bornstein Group at University of Washington. 

Induction of the GST-Fusion Protein (GST-FP)
Batch Purification of the GST-FP using Glutathione (GSH)-Sepharose
Thrombin cleavage of GST-FP to release the recombinant protein
Gel Filtrati ...</description>
            <author>biowww</author>
        </item>
        <item>
            <title>Overcoming the codon bias of E.coli for enhanced protein expression</title>
            <link>http://biowww.net/detail-623.html</link>
            <description>A tech note article (PDF file) discussing codon usage optimization using E.coli plasmid expression system from Novagen Inc. (written by Robert Novy, Don Drott, Keith Yaeger and Robert Mierendorf)

Most amino acids are encoded by more than one codon,and each  ...</description>
            <author>biowww</author>
        </item>
        <item>
            <title>GST-fusion system hints and questions</title>
            <link>http://biowww.net/detail-27.html</link>
            <description>I have been working on purification of proteins using the 
 GST-fusion system for a while, and would like to compile some hints and 
 advice on how to get the highest protein yields. Here are some hints that 
 I have tested that increase the yields for me  ...</description>
            <author>biowww</author>
        </item>
        <item>
            <title>Some guidelines for successful gene expression in E. coli</title>
            <link>http://biowww.net/detail-619.html</link>
            <description>Some guidelines for successful gene expression in E. coli including an overview of the many factors that can influence gene expression such as codon usage, expression vectors, choice of cellular compartment, translocation and folding competence, proteases, and ...</description>
            <author>biowww</author>
        </item>
        <item>
            <title>Recombinant protein expression in Escherichia coli</title>
            <link>http://biowww.net/detail-1058.html</link>
            <description>A open accessible review on recombinant protein expression in E.Coli.

Curr Opin Biotechnol. 1999 Oct;10(5):411-21
François Baneyx

Escherichia coli is one of the most widely used hosts for the production of heterologous proteins and its genetics are far  ...</description>
            <author>biowww</author>
        </item>
        <item>
            <title>Troubleshooting GST fusion protein expression in E. coli</title>
            <link>http://biowww.net/detail-618.html</link>
            <description>By M. Saluta and P. A. Bell, Amersham Pharmacia Biotech.

The production of soluble, intact GST fusion proteins requires optimization of several factors. This discussion focuses on choosing the proper host strain, growth temperature, cell density at time of  ...</description>
            <author>biowww</author>
        </item>
        <item>
            <title>Aggregating protein</title>
            <link>http://biowww.net/detail-131.html</link>
            <description>I have a problem. I am purifying arylamine n-acetyltransferase and 
 the prep is fine until the protein is being concentrated. Around 5 mg/ml the 
 protein seems to aggregate and fall out of solution. Does anybody know any 
 cunning methods to stop proteins ...</description>
            <author>biowww</author>
        </item>
        <item>
            <title>How to express toxic proteins in bacteria</title>
            <link>http://biowww.net/detail-132.html</link>
            <description>I am trying to express my favorite gene cloned in pET vector in 
 E. Coli BL21. The N-terminal truncated protein (missing 13AAs) can be 
 expressed to high level after 1mM IPTG induction for 2 to 4 hours. 
 However the full length protein can not be express ...</description>
            <author>biowww</author>
        </item>
        <item>
            <title>Anaerobic expression of GFP?</title>
            <link>http://biowww.net/detail-144.html</link>
            <description>I'd like to express and His-tag purify GFP expressed preferably in E. coli. But I need to prevent the formation of the chromophore wich is formed by oxidation. ... ...
 
 ...</description>
            <author>biowww</author>
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