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. 2020 Jan 31;10:1570. doi: 10.1038/s41598-020-57775-4

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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(A–D) Schematic representations of the different folding states of apoMb: apoMb at pD 6 ((A) the 8 α-helices are marked with green), apoMb at pD 4 (B), apoMb at pD 2 (C), apoMb denaturated by GdmCl ((D) GdmCl are marked with purple). (E) Cartoon representation of the first non-trivial mode of myoglobin 2v1k.pdb. Loops are marked with green and grey, α-helices with blue, and the motion vectors with red arrows. (F,G) Sketches of a polymer interpreted by the Zimm (F) and ZIF (G) model: the beads are represented by the grey bullets and are interconnected though the springs (blue); additionally, in the ZIF model, the interchain friction is represented through the red dashpot. Each bead interacts with the solvent.