Using a combination of X-ray scattering, fluorescence correlation spectroscopy, coarse-grained molecular dynamics (MD) simulations and potential of mean force calculations, we have explored the membrane remodeling effects of monomeric alpha-synuclein (alpha S). Our initial findings from multiple approaches are that alpha S (1) causes a significant thinning of the bilayer and (2) stabilizes positive mean curvature, such that the maximum principle curvature matches that of synaptic vesicles, alpha S-induced tubules, and the synthetic lipid vesicles to which the protein binds most tightly. This suggests that alpha S binding to synaptic vesicles likely stabilizes their intrinsic curvature. We then show that alpha S induces local negative Gaussian curvature, an effect that occurs in regions of alpha S shown previously via NMR and corroborated by MD simulation to have significant conformational flexibility. The induction of negative Gaussian curvature, which has implications for all curvature-sensing and curvature-generating amphipathic alpha-helices, supports a hypothesis that connects helix insertion to fusion and fission of vesicles, processes that have recently been linked to alpha S function. Then, in an effort to explain these biophysical properties of alpha S, we promote an intrinsic curvature-field model that recasts long-range protein protein interactions in terms of the interactions between the local curvature fields generated by lipid protein complexes.