This title appears in the Scientific Report :
2020
Please use the identifier:
http://dx.doi.org/10.1038/s41598-020-57775-4 in citations.
Please use the identifier: http://hdl.handle.net/2128/24238 in citations.
Transition between protein-like and polymer-like dynamic behavior: Internal friction in unfolded apomyoglobin depends on denaturing conditions
Transition between protein-like and polymer-like dynamic behavior: Internal friction in unfolded apomyoglobin depends on denaturing conditions
Equilibrium dynamics of different folding intermediates and denatured states is strongly connected to the exploration of the conformational space on the nanosecond time scale and might have implications in understanding protein folding. For the first time, the same protein system apomyoglobin has be...
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Personal Name(s): | Balacescu, Livia |
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Schrader, Tobias E. (Corresponding author) / Radulescu, Aurel / Zolnierczuk, Piotr / Holderer, Olaf / Pasini, Stefano / Fitter, Jörg / Stadler, Andreas M. | |
Contributing Institute: |
JCNS-SNS; JCNS-SNS Neutronenstreuung; JCNS-1 Molekulare Biophysik; ICS-5 JCNS-FRM-II; JCNS-FRM-II |
Published in: | Scientific reports, 10 (2020) 1, S. 1570 |
Imprint: |
[London]
Macmillan Publishers Limited, part of Springer Nature
2020
|
DOI: |
10.1038/s41598-020-57775-4 |
PubMed ID: |
32005832 |
Document Type: |
Journal Article |
Research Program: |
Functional Macromolecules and Complexes |
Subject (ZB): | |
Link: |
Get full text Get full text OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/24238 in citations.
Equilibrium dynamics of different folding intermediates and denatured states is strongly connected to the exploration of the conformational space on the nanosecond time scale and might have implications in understanding protein folding. For the first time, the same protein system apomyoglobin has been investigated using neutron spin-echo spectroscopy in different states: native-like, partially folded (molten globule) and completely unfolded, following two different unfolding paths: using acid or guanidinium chloride (GdmCl). While the internal dynamics of the native-like state can be understood using normal mode analysis based on high resolution structural information of myoglobin, for the unfolded and even for the molten globule states, models from polymer science are employed. The Zimm model accurately describes the slowly-relaxing, expanded GdmCl-denaturated state, ignoring the individuality of the different aminoacid side chain. The dynamics of the acid unfolded and molten globule state are similar in the framework of the Zimm model with internal friction, where the chains still interact and hinder each other: the first Zimm relaxation time is as large as the internal friction time. Transient formation of secondary structure elements in the acid unfolded and presence of α-helices in the molten globule state lead to internal friction to a similar extent. |