Issue 24, 2003
From the journal:

Chemical Communications

Functional analysis of the biomimetic silica precipitating activity of the R5 peptide from Cylindrotheca fusiformis†

Marc R. Knechta  and  David W. Wright*a  

* Corresponding authors

a Vanderbilt University, Department of Chemistry, Station B 351822, Nashville, TN 37235-1822, USA
E-mail: David.Wright@vanderbilt.edu
Fax: 615-343-1234
Tel: 615-322-2636

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.

Graphical abstract: Functional analysis of the biomimetic silica precipitating activity of the R5 peptide from Cylindrotheca fusiformis

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Article information

DOI
https://doi.org/10.1039/B309074D
Article type
Communication
Submitted
31 Jul 2003
Accepted
09 Oct 2003
First published
03 Nov 2003

Chem. Commun., 2003, 3038-3039

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Functional analysis of the biomimetic silica precipitating activity of the R5 peptide from Cylindrotheca fusiformis

M. R. Knecht and D. W. Wright, Chem. Commun., 2003, 3038 DOI: 10.1039/B309074D

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