How to fold
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Two novel rare mutations, MCAD842GfiC (R256T) and MCAD 1166AfiG (K364R), have been investigated to assess how far the bio-chemical properties of the mutant proteins correlate with the clinical phenotype of medium chain acyl-CoA dehydrogenase (MCAD) deficiency. When the gene for K364R was overexpressed inEscherichia coli, the syn-thesized mutant protein only exhibited activity when the gene for chapero-nin GroELS was co-overexpressed.
9p fptmusic 12-04-2013 44 2 Download
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Understanding the sequence determinants of protein struc-ture, stabilityand folding is critical for understanding how natural proteins have evolved and how proteins can be engineeredtoperformnovel functions.Thecomplexityof the protein folding problem requires the abilityto search large volumes of sequence space for proteins with specific struc-tural or functional characteristics.
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As more data are generated from proteome and transcriptome analyses of snake venoms, we are gaining an appreciation of the complexity of the venoms and, to some degree, the various sources of such complexity. How-ever, our knowledge is still far from complete.
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The issue of how a newly synthesized polypeptide chain folds to form a protein with a unique three-dimensional structure, otherwise known as the ‘protein-folding problem’, remains a fundamental question in the life sci-ences. Over the last few decades, much information has been gathered about the mechanisms by which proteins fold.
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Opinion Progress towards mapping the universe of protein folds Alastair Grant, David Lee and Christine Orengo Address: Department of Biochemistry and Molecular Biology, University College, Gower Street, London WC1E 6BT, UK. Correspondence: Alastair Grant. E-mail: grant@biochem.ucl.ac.uk comment Published: 29 April 2004 reviews Genome Biology 2004, 5:107 The electronic version of this article is the complete one and can be found online at http://genomebiology.
0p thulanh21 15-11-2011 57 1 Download