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Human plasma fibronectin (Fn) is a large flexible protein stabilized by intermolecular ionic interactions forming a compact structure. On altering solution conditions, the structure can revert to a more expanded state, thereby exposing previously hidden domains (e.g., cell-binding sites). Electron microscopy images of Fn air-sprayed onto mica surfaces show elongated protein structures, indicating a surface-induced structural change. This makes it interesting to investigate the influence of surface properties on the structure of adsorbed Fn. We have used intermittent-contact Atomic Force Microscopy to investigate the structure of Fn adsorbed onto mica, silica, and methylated silica surfaces. We observed that on silica surfaces, which is hydrophilic, most (70%) of the molecules had an elongated structure with partial intramolecular chain interactions, compare to molecules adsorbed on hydrophobic, methylated surfaces, where a compact structure predominated (70%). On mica surfaces, both compact and elongated protein structures were observed, with a slight preference for the elongated form (53%). Results show that surface physical properties influence the molecular structure of fibronectin on adsorption, which could provide useful information in understanding surface-induced in vivo responses.