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Stability and activity modulation of chymotrypsins in AOT reversed micelles by protein-interface interaction. Interaction of a-chymotrypsin with a negative interface leads to a cooperative breakage of a salt bridge that keeps the catalytic active conformation (Ile16-Asp194)


Stability and activity modulation of chymotrypsins in AOT reversed micelles by protein-interface interaction. Interaction of a-chymotrypsin with a negative interface leads to a cooperative breakage of a salt bridge that keeps the catalytic active conformation (Ile16-Asp194)



Biotechnology and Bioengineering 59(3): 0-3



ISSN/ISBN: 0006-3592


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Accession: 018125962

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Related references

Stability and activity modulation of chymotrypsins in AOT reversed micelles by protein-interface interaction: interaction of alpha-chymotrypsin with a negative interface leads to a cooperative breakage of a salt bridge that keeps the catalytic active conformation (Ile16-Asp194). Biotechnology and Bioengineering 59(3): 360-363, 1998

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