Functional analysis of the biomimetic silica precipitating activity of the R5 peptide from Cylindrotheca fusiformis.
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.
Knecht
Marc R
MR
Vanderbilt University, Department of Chemistry, Station B 351822, Nashville, TN 37235-1822, USA.
Wright
David W
DW
D000595:Amino Acid Sequence; D040761:Biomimetic Materials / Q000737:chemistry; D011232:Chemical Precipitation; D017377:Diatoms / Q000737:chemistry*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010316:Particle Size; D010455:Peptides / Q000032:analysis / Q000737:chemistry*; D012822:Silicon Dioxide / Q000737:chemistry*; D013055:Spectrophotometry, Infrared
D010455:Peptides; D012822:Silicon Dioxide