title: Thermal unfolding of myoglobin in the Landau-Ginzburg-Wilson approach.
abstract: 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 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.
authors.affiliation: Department of Physics and Astronomy, University of British Columbia, Vancouver, British Columbia V6T1Z4, Canada.
authors.forename: Xubiao
authors.initials: X
authors.lastname: Peng
authors.affiliation: Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, 80-308 Gdańsk, Poland.
authors.forename: Adam K
authors.initials: AK
authors.lastname: Sieradzan
authors.affiliation: Department of Physics and Astronomy, Uppsala University, P. O. Box 803, S-75108, Uppsala, Sweden.|Laboratoire de Mathematiques et Physique Theorique CNRS UMR 6083, Fédération Denis Poisson, Université de Tours, Parc de Grandmont, F37200, Tours, France.|Department of Physics, Beijing Institute of Technology, Haidian District, Beijing 100081, People's Republic of China.
authors.forename: Antti J
authors.initials: AJ
authors.lastname: Niemi
mesh_terms: D008954:Models, Biological; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D009211:Myoglobin