Biomimetic silica forrnation, a process that is largely driven by proteins, has garnered considerable interest in recent years due to its role in the development Of new biotechnologies. However, much remains unknown of the molecular-scale mechanisms underlying the binding of proteins to biomineral surfaces such as silica, or even of the key residue-level interactions between,such proteins and surfaces. In this study, we employ molecular dynamics (MD) simulations to study the binding of R5 a 19-residue segment of a native silaffin peptide used for in vitro silica formation-to a silica surface. The metaclynamics enhanced Sampling methd is used to converge the binding behavior of R5 on silica at both neutral (pH 7.5) and acidic (pH 5) conditions. The results show fundamental differences in the mechanism of binding between the two cases, providing unique insight into the pH dependent ability of R5 and native silaffin to precipitate silica. We also study the effect of phosphorylation of serine residues in R5 on both the binding free energy to silica and the interfacial conformation of the peptide. Results indicate that phosphorylation drastically decreases the binding free energy and changes the structure of silica-adsorbed R5 through the introduction of charge and steric repulsion. New mechanistic insights from this work could inform rational design of new biomaterials and biotechnologies.