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Abstract
Cathepsin L mutants with the ability to condense silica from solution have been generated and a 1.5 angstrom crystal structure of one of these chimeras allows us to rationalise the catalytic mechanism of silicic acid condensation.
| Original language | English |
|---|---|
| Pages (from-to) | 1765-1767 |
| Number of pages | 3 |
| Journal | Chemical Communications |
| Issue number | 15 |
| DOIs | |
| Publication status | Published - 21 Apr 2008 |
Keywords
- DEMOSPONGE SUBERITES-DOMUNCULA
- HUMAN PROCATHEPSIN L
- IN-VITRO
- BIOSILICA
- FILAMENTS
- SPICULES
- BIOLOGY
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Dive into the research topics of 'Crystal structure and silica condensing activities of silicatein alpha-cathepsin L chimeras'. Together they form a unique fingerprint.Projects
- 1 Finished
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BBSRC BBS/B/14426: SPORT
Naismith, J. (PI)
Biotechnology and Biological Sciences Research Council
18/10/04 → 30/04/12
Project: Standard