Amyloid proteins are an atypical product of gene translation, characterised by an innate tendency to polymerize into insoluble fibrillar aggregates. The formation of amyloid fibres is commonly associated with detrimental cellular effects, and is most prominently recognised as a hallmark of several human neurodegenerative disorders. However, despite the risk of aggregation-induced cytotoxicity, many organisms have evolved to exploit the unique physicochemical properties of these fibres. Indeed, these "functional" amyloids operate in a host of diverse roles, including; protein storage, melanin production, and extracellular matrix formation. The first functional amyloid to be identified was the Curli fimbriae of Escherichia coli. This extracellularly secreted fibre forms the main proteinaceous component of its biofilm, providing it with a protective shell. Extensive study of this system has revealed a stringently coordinated assembly mechanism, under the regulation of two divergently transcribed operons. More recently, another such biofilm amyloid was identified in the Pseudomonas genus - the Functional Amyloid Protein (FAP) operon. Whilst Fap fibres are morphologically similar to their Curli counterparts, the gene organisation and proteins involved are distinct. Work in this thesis seeks to characterise a range of proteins within the Fap operon, with particular focus on those that are structural components of the fibre - FapB, FapC, and FapE. Using solution state NMR, structural propensity and dynamics were found to differ between the disordered pre-fibre states of FapB and FapC. The Curli amyloid protein, CsgA, was also studied in pre-fibrillar state, identifying the effect of the N-terminal 22 residues in stabilising the monomer, and highlighting the importance of the prion-like motifs in amyloid formation. Furthermore, previous results in our lab have shown that curli-specific gene C (CsgC) potently inhibits CsgA/FapC amyloid formation, via transient electrostatic interactions. In continuation of this work, here I explore other distantly related CsgC-like sequences in an effort to elucidate the structural traits that are important in stalling amyloidogenesis.