Our analysis, based on a membrane-coupled anisotropic network model, reveals two types of NCT motions, bending and twisting, with respect to PS1.
Our analysis of the 2-unit model reveals four types of qualitative dynamics observed in the model: Type I: The state vector converges to a unique equilibrium in which only unit 1 is active.
Second, they can defend a version of perspectival realism (Giere 1999, Rueger 2005) according to which each model reveals one aspect of the phenomenon in question, and when taken together a full (or fuller) account emerges.
The growth model reveals two interesting results.
Their refined model reveals two major domains - a prototypical α/β hydrolase fold derived from two non-contiguous stretches of the protein and a novel helical bundle (referred to as an SKS domain by the authors) that serves to cap the active site.
The model revealed three distinct growth phases.
Based on several reports showing only 1 1 stochiometry for LysM domains in the past, we performed ITC measurements and were able to fit the data to a "one binding site" model, revealing three binding sites for these oligosaccharides per Ecp6 molecule.
The free-ratio model revealed three specific branches having ω > 1: the branch ancestral to P. fieldi and P. vivax (branch A, ω1), the branch ancestral to branch A and P. cynomolgi (branch B, ω2), and the branch ancestral to P. hylobari and P. inui (branch C, ω3).
