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 |
|---|---|
| Pages (from-to) | 3038-3039 |
| Number of pages | 2 |
| Journal | Chemical Communications |
| Volume | 9 |
| Issue number | 24 |
| State | Published - Dec 21 2003 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Chemistry(all)
Cite this
Functional analysis of the biomimetic silica precipitating activity of the R5 peptide from Cylindrotheca fusiformis. / Knecht, Marc; Wright, David W.
In: Chemical Communications, Vol. 9, No. 24, 21.12.2003, p. 3038-3039.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Functional analysis of the biomimetic silica precipitating activity of the R5 peptide from Cylindrotheca fusiformis
AU - Knecht, Marc
AU - Wright, David W.
PY - 2003/12/21
Y1 - 2003/12/21
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0346250119&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0346250119&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0346250119
VL - 9
SP - 3038
EP - 3039
JO - Chemical Communications
JF - Chemical Communications
SN - 1359-7345
IS - 24
ER -