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Thermal unfolding of myoglobin in the Landau-Ginzburg-Wilson approach
Univ British Columbia, Dept Phys & Astron, Vancouver, BC V6T 1Z4, Canada..
Univ Gdansk, Fac Chem, Wita Stwosza 63, PL-80308 Gdansk, Poland..
Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy, Theoretical Physics. Univ Tours, Lab Math & Phys Theor, CNRS UMR 6083, Federat Denis Poisson, Parc Grandmont, F-37200 Tours, France.;Beijing Inst Technol, Dept Phys, Beijing 100081, Peoples R China..
2016 (English)In: Physical review. E, ISSN 2470-0045, E-ISSN 2470-0053, Vol. 94, no 6, 062405Article in journal (Refereed) Published
Abstract [en]

The Landau-Ginzburg-Wilson paradigm is applied to model the low-temperature crystallographic C alpha 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 alpha-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 characterize 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
American Physical Society, 2016. Vol. 94, no 6, 062405
National Category
Physical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-323683DOI: 10.1103/PhysRevE.94.062405ISI: 000400692900003OAI: oai:DiVA.org:uu-323683DiVA: diva2:1106987
Available from: 2017-06-08 Created: 2017-06-08 Last updated: 2017-06-08Bibliographically approved

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