Humanistische Betrachtungen und Gegenwart

  The Geometrical Architecture of Tau: Assessing Structural Domain Organization via Fibonacci, Lucas, and Midpoint Proportions   - A First Look by Stefan Geier, Katharina Geier et al., ISTS Simssee, Gerhart-Hauptmann-Strasse 6, 83071 Stephanskirchen Abstract Human microtubule-associated protein tau (MAPT) exists as a structural shapeshifter, expressed in the adult central nervous system as six distinct alternative-spliced isoforms ranging from 352 to 441 amino acids. While traditional structural biology treats tau as an intrinsically disordered protein (IDP) governed strictly by stochastic conformational ensembles, this paper explores an alternative, appreciative paradigm: the striking mathematical alignment of tau's isoform lengths and domain boundaries with the Fibonacci ( $F_n$ ) and Lucas ( $L_n$ ) sequences, alongside their mathematical midpoints. Rather than dismissing these matches as numerological artifacts, we highlight how these recurring integer series provide ...

  A Structural Assessment of Human Alpha-Synuclein Domains: Testing Correlations with Fibonacci, Lucas, and Midpoint Sequences - A First Look by Stefan Geier, Katharina Geier et al., ISTS Simssee, Gerhart-Hauptmann-Strasse 6, 83071 Stephanskirchen Abstract Human alpha-synuclein ( $\alpha$ -syn) is a 140-amino-acid intrinsically disordered protein heavily implicated in Parkinson’s disease pathology. While numerical alignments between its structural domains and mathematical sequences (such as Fibonacci, Lucas, and their midpoints) can be generated, this paper evaluates whether these correlations represent an underlying biological principle or a stochastic artifact. Our analysis demonstrates that while $\alpha$ -syn’s domain lengths are constrained by functional, lipid-binding amphipathic motifs, matches to integer sequences lack selective evolutionary mechanisms and are primarily the product of mathematical curve-fitting. 1. Introduction Alpha-synuclein ( $\alpha$ -syn) plays a centr...