Authors:	Lüdeke, Steffen Lohner, Philipp Stühn, Lara G. Betschart, Martin U. Huber, Matthias C. Schreiber, Andreas Schiller, Stefan M.
Title:	Dynamic structural changes and thermodynamics in phase separation processes of an intrinsically disordered–ordered protein model
Online publication date:	24-Oct-2022
Year of first publication:	2022
Language:	english
Abstract:	Elastin-like proteins (ELPs) are biologically important proteins and models for intrinsically disordered proteins (IDPs) and dynamic structural transitions associated with coacervates and liquid–liquid phase transitions. However, the conformational status below and above coacervation temperature and its role in the phase separation process is still elusive. Employing matrix least-squares global Boltzmann fitting of the circular dichroism spectra of the ELPs (VPGVG)20, (VPGVG)40, and (VPGVG)60, we found that coacervation occurs sharply when a certain number of repeat units has acquired β-turn conformation (in our sequence setting a threshold of approx. 20 repeat units). The character of the differential scattering of the coacervate suspensions indicated that this fraction of β-turn structure is still retained after polypeptide assembly. Such conformational thresholds may also have a role in other protein assembly processes with implications for the design of protein-based smart materials.
DDC:	540 Chemie 540 Chemistry and allied sciences
Institution:	Johannes Gutenberg-Universität Mainz
Department:	FB 09 Chemie, Pharmazie u. Geowissensch.
Place:	Mainz
ROR:	https://ror.org/023b0x485
DOI:	http://doi.org/10.25358/openscience-8023
Version:	Published version
Publication type:	Zeitschriftenaufsatz
License:	CC BY
Information on rights of use:	https://creativecommons.org/licenses/by/4.0/
Journal:	Angewandte Chemie 61 3
Pages or article number:	e202112738
Publisher:	Wiley-VCH
Publisher place:	Weinheim
Issue date:	2022
ISSN:	1521-3773
Publisher DOI:	10.1002/anie.202112738
Appears in collections:	JGU-Publikationen