Topology to geometry in protein folding: β-Lactoglobulin

摘要: Evolution of protein structure from random coil to native is first represented topologically by its time-dependent sequences discretized Ramachandran basins occupied successive backbone residues. Introducing energetic and entropic criteria at each instant observation transforms the description a structurally ambiguous topological representation an unambiguous geometric picture folding process. The method applied with success β-lactoglobulin, traditionally perplexing because reputed nonhierarchical pattern. This molecule passes through stage, ca. 0.1 μs duration, transient, “flickering” α-helical structure, until bit tertiary forms that stabilizes system long enough allow it pass β-sheet.