Abstract
A synthetic site-directed mutagenesis study of the non post- translationally modified silica precipitating R5 peptide reveals that the RRIL motif is critical in the formation of active silica precipitating assemblies.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3038-3039 |
| Number of pages | 2 |
| Journal | Chemical Communications |
| Volume | 3 |
| Issue number | 24 |
| DOIs | |
| State | Published - Jan 1 2003 |
| Externally published | Yes |
ASJC Scopus subject areas
- Catalysis
- Electronic, Optical and Magnetic Materials
- Ceramics and Composites
- Chemistry(all)
- Surfaces, Coatings and Films
- Metals and Alloys
- Materials Chemistry
Fingerprint Dive into the research topics of 'Functional analysis of the biomimetic silica precipitating activity of the R5 peptide from Cylindrotheca fusiformis'. Together they form a unique fingerprint.
Cite this
Knecht, M. R., & Wright, D. W. (2003). Functional analysis of the biomimetic silica precipitating activity of the R5 peptide from Cylindrotheca fusiformis. Chemical Communications, 3(24), 3038-3039. https://doi.org/10.1039/b309074d