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Crystal structure and silica condensing activities of silicatein alpha-cathepsin L chimeras.


ABSTRACT: Cathepsin L mutants with the ability to condense silica from solution have been generated and a 1.5 A crystal structure of one of these chimeras allows us to rationalise the catalytic mechanism of silicic acid condensation.

SUBMITTER: Fairhead M 

PROVIDER: S-EPMC3326524 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature

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Crystal structure and silica condensing activities of silicatein alpha-cathepsin L chimeras.

Fairhead Michael M   Johnson Kenneth A KA   Kowatz Thomas T   McMahon Stephen A SA   Carter Lester G LG   Oke Muse M   Liu Huanting H   Naismith James H JH   van der Walle Christopher F CF  

Chemical communications (Cambridge, England) 20080211 15


Cathepsin L mutants with the ability to condense silica from solution have been generated and a 1.5 A crystal structure of one of these chimeras allows us to rationalise the catalytic mechanism of silicic acid condensation. ...[more]

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