Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change.
| Title: | Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change. |
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| Authors: | Fonin AV; Institute of Cytology of the Russian Academy of Sciences, Laboratory of Structural Dynamics, Stability and Folding of Proteins, Tikhoretsky av. 4, St. Petersburg, Russia.; Stepanenko OV; Institute of Cytology of the Russian Academy of Sciences, Laboratory of Structural Dynamics, Stability and Folding of Proteins, Tikhoretsky av. 4, St. Petersburg, Russia.; Sitdikova AK; Institute of Cytology of the Russian Academy of Sciences, Laboratory of Structural Dynamics, Stability and Folding of Proteins, Tikhoretsky av. 4, St. Petersburg, Russia.; Antifeeva IA; Institute of Cytology of the Russian Academy of Sciences, Laboratory of Structural Dynamics, Stability and Folding of Proteins, Tikhoretsky av. 4, St. Petersburg, Russia.; Kostyleva EI; Institute of Cytology of the Russian Academy of Sciences, Laboratory of Structural Dynamics, Stability and Folding of Proteins, Tikhoretsky av. 4, St. Petersburg, Russia.; Polyanichko AM; Saint-Petersburg State University, Physical Faculty, Universitetskaya nab., 7-9, St. Petersburg, Russia.; Karasev MM; University of Helsinki, Faculty of Medicine, Haartmaninkatu 8, Helsinki, Finland.; Silonov SA; Institute of Cytology of the Russian Academy of Sciences, Laboratory of Structural Dynamics, Stability and Folding of Proteins, Tikhoretsky av. 4, St. Petersburg, Russia.; Povarova OI; Institute of Cytology of the Russian Academy of Sciences, Laboratory of Structural Dynamics, Stability and Folding of Proteins, Tikhoretsky av. 4, St. Petersburg, Russia.; Kuznetsova IM; Institute of Cytology of the Russian Academy of Sciences, Laboratory of Structural Dynamics, Stability and Folding of Proteins, Tikhoretsky av. 4, St. Petersburg, Russia.; Uversky VN; University of South Florida, Morsani College of Medicine, Department of Molecular Medicine and Byrd Alzheimer's Research Institute, FL 33612, Tampa, USA. Electronic address: vuversky@health.usf.edu.; Turoverov KК; Institute of Cytology of the Russian Academy of Sciences, Laboratory of Structural Dynamics, Stability and Folding of Proteins, Tikhoretsky av. 4, St. Petersburg, Russia; Peter the Great St. Petersburg Polytechnic University, Department of Biophysics, Polytechnicheskaya av. 29, St. Petersburg, Russia. Electronic address: kkt@incras.ru. |
| Source: | International journal of biological macromolecules [Int J Biol Macromol] 2019 Mar 15; Vol. 125, pp. 244-255. Date of Electronic Publication: 2018 Dec 05. |
| Publication Type: | Journal Article |
| Language: | English |
| Journal Info: | Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE |
| Imprint Name(s): | Publication: Amsterdam : Elsevier; Original Publication: Guildford, Eng., IPC Science and Technology Press. |
| MeSH Terms: | Hydrogen-Ion Concentration* ; Protein Folding*; Amino Acids/*chemistry ; Intrinsically Disordered Proteins/*chemistry ; Peptides/*chemistry; Amyloid/chemistry ; Intrinsically Disordered Proteins/isolation & purification ; Peptides/isolation & purification ; Polyethylene Glycols/chemistry ; Protein Conformation ; Spectrum Analysis |
| Abstract: | pH-induced structural changes of the synthetic homopolypeptides poly-E, poly-K, poly-R, and intrinsically disordered proteins (IDPs) prothymosin α (ProTα) 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-α-helix transition of ProTα 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.; (Copyright © 2018 Elsevier B.V. All rights reserved.) |
| Substance Nomenclature: | 0 (Amino Acids); 0 (Amyloid); 0 (Intrinsically Disordered Proteins); 0 (Peptides); 3WJQ0SDW1A (Polyethylene Glycols) |
| Entry Date(s): | Date Created: 20181212 Date Completed: 20190521 Latest Revision: 20190521 |
| Update Code: | 20260130 |
| DOI: | 10.1016/j.ijbiomac.2018.12.038 |
| PMID: | 30529354 |
| Database: | MEDLINE |
Journal Article