In this study we demonstrate that NMR can be used to characterize the structure of AgA, an adhesin involved in the sucrose-independent attachment of S. mutans. Preliminary studies of AgA failed to optimize the production and purification of the protein which manifested as two bands at a close molecular weight in an SDS-PAGE of the final sample. A preliminary 15N-1H-HSQC was done of the impure sample and indicated a dispersed pattern. We would like to improve the HSQC by optimizing the protocol for the production and purification of AgA. We used 13C/15N-NMR to assign the amino acid residues of AgA and developed an NMR-based approach for future studies of the protein. An assignment of the protein will improve the understanding of the protein structure. This information can be used for further studies of AgA and its role in amyloid formation, such as when studying the interaction between AgA and another wall adhesin protein like P1 that has also been implicated in biofilm formation. This knowledge can be applied to using AgA as a potential target of biofilm inhibition to improve treatment of dental caries.