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Alpha-lytic protease

Sohl J. L, Jaswal S. S. and Agard D. A. Unfolded conformations of alpha-lytic protease are more stable than its native state. Nature (1998) 395(6704) ... [Pg.101]

Hunkapillar, M. W., Smallcombe, S. H., Whitaker, D. R., and Richards,J. H. (1973). Carbon NMR studies of the histidine residue in alpha-lytic protease. Implication for the mechanism of serine proteases. Biochemistry 12,4732-4743. [Pg.83]

Interaction of M.c. with a polypeptide is normally considered to be noncovalent. However, the definition may be extended to include special cases of covalently bound M.c. such as the pro-sequence of pro-subtilisin and alpha-lytic protease, and the ubiquitin sequence at the aminoterminus of 2-iibosomal precursor proteins in eukaryotes. In each of these cases. [Pg.410]

Ivanov, D. Bachovchin, W. W. Redfield, A. G. Boron-11 pure quadrupole resonance investigation of peptide boronic acid inhibitors bound to alpha-lytic protease. Biochemistry 2002, 41, 1587—1590. [Pg.236]


See other pages where Alpha-lytic protease is mentioned: [Pg.358]    [Pg.77]    [Pg.74]   
See also in sourсe #XX -- [ Pg.362 ]




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