Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change

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Fonin , A V , Stepanenko , O V , Sitdikova , A K , Antifeeva , I A , Kostyleva , E I , Polyanichko , A M , Karasev , M M , Silonov , S A , Povarova , O I , Kuznetsova , I M , Uversky , V N & Turoverov , K K 2019 , ' Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change ' , International Journal of Biological Macromolecules , vol. 125 , pp. 244-255 . https://doi.org/10.1016/j.ijbiomac.2018.12.038

Title: Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change
Author: Fonin, Alexander V.; Stepanenko, Olga V.; Sitdikova, Asiia K.; Antifeeva, Iuliia A.; Kostyleva, Elena I.; Polyanichko, Alexander M.; Karasev, Maksim M.; Silonov, Sergey A.; Povarova, Olga I.; Kuznetsova, Irina M.; Uversky, Vladimir N.; Turoverov, Konstantin K.
Contributor organization: Medicum
Date: 2019-03-15
Language: eng
Number of pages: 12
Belongs to series: International Journal of Biological Macromolecules
ISSN: 0141-8130
DOI: https://doi.org/10.1016/j.ijbiomac.2018.12.038
URI: http://hdl.handle.net/10138/312558
Abstract: pH-induced structural changes of the synthetic homopolypeptides poly-E, poly-K, poly-R, and intrinsically disordered proteins (IDPs) prothymosin alpha (ProT alpha) and linker histone H1, in concentrated PEG solutions simulating macromolecular crowding conditions within the membrane-less organelles, were characterized. The conformational transitions of the studied poly-amino acids in the concentrated PEG solutions depend on the polymerization degree of these homopolypeptides, the size of their side chains, the charge distribution of the side chains, and the crowding agent concentration. The results obtained for poly-amino acids are valid for IDPs having a significant total charge. The overcrowded conditions promote a significant increase in the cooperativity of the pH-induced coil-alpha-helix transition of ProTa and provoke histone H1 aggregation. The most favorable conditions for the pH-induced structural transitions in concentrated PEG solutions are realized when the charged residues are grouped in blocks, and when the distance between the end of the side group carrying charge and the backbone is small. Therefore, the block-wise distribution of charged residues within the IDPs not only plays an important role in the liquid-liquid phase transitions, but may also define the expressivity of structural transitions of these proteins in the overcrowded conditions of the membrane-less organelles. (C) 2018 Elsevier B.V. All rights reserved.
Subject: HELIX-COIL TRANSITION
PHASE-SEPARATION
PROTHYMOSIN-ALPHA
TERMINAL DOMAIN
CONFORMATIONAL TRANSITIONS
THERMODYNAMIC PARAMETERS
SECONDARY STRUCTURE
POLYPEPTIDE-CHAINS
STABILITY
STATE
1182 Biochemistry, cell and molecular biology
3111 Biomedicine
Peer reviewed: Yes
Rights: unspecified
Usage restriction: openAccess
Self-archived version: publishedVersion


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