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Thermal unfolding of myoglobin in the Landau-Ginzburg-Wilson approach
Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy, Theoretical Physics.
2016 (English)Article in journal (Other academic) Submitted
Abstract [en]

The Landau-Ginzburg-Wilson paradigm is applied to model the low-temperature crystallographic Cα backbone structure of sperm whale myoglobin. The Glauber protocol is employed to simulate its response to an increase in ambient temperature. The myoglobin is found to unfold from its native state by a succession of α-helical intermediates, fully in line with the observed folding and unfolding patterns in denaturation experiments. In particular, a molten globule intermediate is identified with experimentally correct attributes. A detailed, experimentally testable contact map is constructed to characterise the specifics of the unfolding pathway, including the formation of long range interactions. The results reveal how the unfolding process of a protein is driven by the interplay between, and a successive melting of, its modular secondary structure components.

Place, publisher, year, edition, pages
National Category
Subatomic Physics
Research subject
Theoretical Physics
URN: urn:nbn:se:uu:diva-287911OAI: oai:DiVA.org:uu-287911DiVA: diva2:923585
Available from: 2016-04-26 Created: 2016-04-26 Last updated: 2016-04-26

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Niemi, Antti
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