Topology to Geometry in Protein Folding: β-Lactoglobulin

Evolution of protein structure from random coil to native is first represented topologically by its time-dependent sequences of discretized Ramachandran basins occupied by successive backbone residues. Introducing energetic and entropic criteria at each instant of observation transforms the descript...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2000-12, Vol.97 (26), p.14062-14066
Main Authors: Fernández, A, Colubri, A, Berry, R S
Format: Article
Language:English
Subjects:
Ambiguity
Biological Sciences
Biology
Chemistry
Computer Simulation
Entropy
Free energy
Geometric topology
Geometry
Kinetics
Lactoglobulins - chemistry
Models, Molecular
Physical Sciences
Physics
Protein Folding
Protein Structure, Secondary
Proteins
Protons
Topological vector spaces
Topology
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Summary:Evolution of protein structure from random coil to native is first represented topologically by its time-dependent sequences of discretized Ramachandran basins occupied by successive backbone residues. Introducing energetic and entropic criteria at each instant of observation transforms the description from a structurally ambiguous topological representation to an unambiguous geometric picture of the folding process. The method is applied with success to folding of β-lactoglobulin, traditionally perplexing because of its reputed nonhierarchical folding pattern. This molecule passes through a stage, ca. 0.1 μs duration, of transient, "flickering" α-helical structure, until a bit of tertiary structure forms that stabilizes the system long enough to allow it to pass to its native β-sheet.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.260359997