Cloning, purification and biophysical characterization of the IgA1 protease associated [alpha]-proteins from Neisseria gonorrhoeae  and Neisseria meningitidis.
Published: 2004
Language: eng
Number of pages: 101
Description: The IgA1 protease associated alpha-proteins carry nuclear localizing signals and are putative virulence factors found only in pathogenic  Neisseria. The alpha-proteins from Neisseria gonorrhoeae  strain MS11 (alphaG) and Neisseria meningitidis strain Z2491 (alphaM) have been produced in a bacterial expression system and purified with high yields. They are biophysically characterized here. Far-UV circular dichroism spectroscopy indicated these proteins are 60% alpha-helical at 25&deg;C and undergo a cooperative transition during thermal denaturation with a melting point of 42&deg;C. The a-proteins are found to exist as highly extended monomeric species in solution with a proteolytically resistant core domain at the C-terminal half of the molecule while the N-terminal region forms an extended tail that is intrinsically disordered. NMR analysis of these proteins suggests that even the compact C-terminal domain is structurally unstable and in slow exchange between different conformations.
Notes: Adviser:  Emil F. Pai.

Thesis (M.Sc.)--University of Toronto, 2004.

Electronic version licensed for access by U. of T. users.

Source: Masters Abstracts International, Volume: 42-06, page: 2206.

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