Ray, Soumya S and Balaram, Hemalatha and Balaram, P (1999) Unusual stability of a multiply nicked form of Plasmodium falciparum triosephosphate isomerase. In: Chemistry and Biology, 6 (9). pp. 625-637.
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The limited proteolytic cleavage of proteins can result in distinct polypeptides that remain noncovalently associated so that the structural and biochemical properties of the ‘nicked’ protein are virtually indistinguishable from those of the native protein. The remarkable observation that rabbit muscle triosephosphate isomerase (TIM) can be multiply nicked by subtilisin and efficiently religated in the presence of an organic solvent formed the stimulus for our study on a homologous system, Plasmodium falciparum triosephosphate isomerase (PfTIM).
|Item Type:||Journal Article|
|Additional Information:||copyright of thia article belongs to Elsevier B.V.|
|Keywords:||folding;ligation;mass spectrometry;triosephosphate isomerase|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||10 Oct 2007|
|Last Modified:||19 Sep 2010 04:40|
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