arXiv subjects

Sijung Yun

Publications and source records attributed to Sijung Yun.

2 recordsLinked to original sources

arXiv2025

W3ID: A Quantum Computing-Secure Digital Identity System Redefining Standards for Web3 and Digital Twins

The rapid advancements in quantum computing present significant threats to existing encryption standards and internet security. Simultaneously, the advent of Web 3.0 marks a transformative era in internet history, emphasizing enhanced data security, decentralization, and user ownership. This white paper introduces the W3ID, an abbreviation of Web3 standard meeting universal digital ID, which is a Universal Digital Identity (UDI) model designed to meet Web3 standards while addressing vulnerabilities posed by quantum computing. W3ID innovatively generates secure Digital Object Identifiers (DOIs) tailored for the decentralized Web 3.0 ecosystem. Additionally, W3ID employs a dual-key system for secure authentication, enhancing both public and private verification mechanisms. To further enhance encryption strength and authentication integrity in the quantum computing era, W3ID incorporates an advanced security mechanism. By requiring quadruple application of SHA-256, with consecutive matches for validation, the system expands the number of possibilities to 256^4, which is approximately 4.3 billion times the current SHA-256 capacity. This dramatic increase in computational complexity ensures that even advanced quantum computing systems would face significant challenges in executing brute-force attacks. W3ID redefines digital identity standards for Web 3.0 and the quantum computing era, setting a new benchmark for security, scalability, and decentralization in the global digital twin ecosystem.

cs.CR↗

arXiv2007

Role of electrostatic interactions in amyloid beta-protein (Abeta) oligomer formation: A discrete molecular dynamics study

Pathological folding and oligomer formation of the amyloid beta-protein (Abeta) are widely perceived as central to Alzheimer's disease (AD). Experimental approaches to study Abeta self-assembly are problematic, because most relevant aggregates are quasi-stable and inhomogeneous. We apply a discrete molecular dynamics (DMD) approach combined with a four-bead protein model to study oligomer formation of the amyloid beta-protein (Abeta). We address the differences between the two most common Abeta alloforms, Abeta40 and Abeta42, which oligomerize differently in vitro. We study how the presence of electrostatic interactions (EIs) between pairs of charged amino acids affects Abeta40 and Abeta42 oligomer formation. Our results indicate that EIs promote formation of larger oligomers in both Abeta40 and Abeta42. The Abeta40 size distribution remains unimodal, whereas the Abeta42 distribution is trimodal, as observed experimentally. Abeta42 folded structure is characterized by a turn in the C-terminus that is not present in Abeta40. We show that the same C-terminal region is also responsible for the strongest intermolecular contacts in Abeta42 pentamers and larger oligomers. Our results suggest that this C-terminal region plays a key role in the formation of Abeta42 oligomers and the relative importance of this region increases in the presence of EIs. These results suggest that inhibitors targeting the C-terminal region of Abeta42 oligomers may be able to prevent oligomer formation or structurally modify the assemblies to reduce their toxicity.

q-bio.BM↗