Abstract
The HMG domain is a DNA binding and bending ‘architectural’ motif involved in chromatin re-modelling during transcription. Recombinant SRY HMG domain protein, 88 amino acids in length, has been produced in E. coli. Using FPLC and a stirred ultra-filtration cell, this domain has been purified to homogeneity and concentrated to yield milligram quantities. Functional characterisation studies of the pure, concentrated SRY HMG domain show the recombinantly expressed protein to be active in terms of DNA binding and calmodulin binding activities.
Keywords: hmg, sry hmg domain, recombinant protein expression, fplc purification, mass spectrometry, dna binding
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