title: Functional analysis of the biomimetic silica precipitating activity of the R5 peptide from Cylindrotheca fusiformis.
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.
authors.affiliation: Vanderbilt University, Department of Chemistry, Station B 351822, Nashville, TN 37235-1822, USA.
authors.forename: Marc R
authors.initials: MR
authors.lastname: Knecht
authors.forename: David W
authors.initials: DW
authors.lastname: Wright
mesh_terms: 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
chemical_list: D010455:Peptides; D012822:Silicon Dioxide