We present the first application of the recently developed Basis Light-Front Quantization (BLFQ) method to self-bound systems in quantum field theory, using the positronium system as a test case. Within the BLFQ framework, we develop a two-body effective interaction, operating only in the lowest Fock sector, that implements photon exchange, neglecting fermion self-energy effects. We then solve for the mass spectrum of this interaction at the unphysical coupling α = 0.3. The resulting spectrum is in good agreement with the expected Bohr spectrum of non-relativistic quantum mechanics. We examine in detail the dependence of the results on the regulators of the theory.

We extend the idea of weak measurements to the general case, provide a complete treatment and obtain results for both the regime when the pre-selected and post-selected states (PPS) are almost orthogonal and the regime when they are exactly orthogonal. We surprisingly find that for a fixed interaction strength, there may exist a maximum signal amplification and a corresponding optimum overlap of PPS to achieve it. For weak measurements in the orthogonal regime, we find interesting quantities that play the same role that weak values play in the non-orthogonal regime.

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More than 20 human diseases, including Alzheimer's disease, Parkinson's disease, and prion disease, originate from the deposition of misfolded proteins. These proteins, referred as amyloidogenic proteins, adopt a β-sheet-rich structure when transformed from soluble state into insoluble amyloid fibrils. Amyloid formation is influenced by a number of factors that affect the intermolecular interaction, including pH, temperature, ion strength, and chemical bonds. In this review, we focus on the role of disulfide on the stability, structure, oligomerization, and amyloidogenecity of native folded or unfolded amyloidogenic proteins. The effects of introduced disulfide bonds on the amyloidogenicity of proteins lacking native disulfide are also reviewed.

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