Abstract:
:The recombinant catalytic subunit of human protein kinase CK2 bas been mutagenised at the C-terminal region in an attempt to induce this tail to fold. We suppose in fact that this unstructured C-terminus just might be responsible for the high degradability of the human enzyme. On the basis of theoretical calculations we choose to substitute two distal prolines with alanines (PA 382-384). The mutant bas been purified to the electrophoretic homogeneity by means of three chromatographic steps. By circular dichroism Spectroscopy we verified if the double amino acids substitution reflected on the secondary structure of the recombinant a subunit. According to our theoretical predictions, we observed that the alpha-helix content of the protein increased when the two distal prolines were substituted by alanines. Moreover the mutant catalytic subunit shows a reduced ability to bind a classical inhibitor such as heparin.
journal_name
Mol Biol Repjournal_title
Molecular biology reportsauthors
Grasselli E,Noviello G,Rando C,Nicolini C,Vergani Ldoi
10.1023/a:1023934805326keywords:
subject
Has Abstractpub_date
2003-06-01 00:00:00pages
97-106issue
2eissn
0301-4851issn
1573-4978journal_volume
30pub_type
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