TY - JOUR

T1 - Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change.

AU - Fonin, A.V.

AU - Stepanenko, O.V.

AU - Sitdikova, A.K.

AU - Antifeeva, I.A.

AU - Kostyleva, E.I.

AU - Polyanichko, A.M.

AU - Karasev, M.M.

AU - Silonov, S.A.

AU - Povarova, O.I.

AU - Kuznetsova , I.M.

AU - Uversky, V.N.

AU - Turoverov, K.K.

N1 - 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. (2018) Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change. International Journal of Biological Macromolecules.(DOI: 10.1016/j.ijbiomac.2018.12.038)

PY - 2019/3/15

Y1 - 2019/3/15

N2 - 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.

AB - 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.

KW - CONFORMATIONAL TRANSITIONS

KW - HELIX-COIL TRANSITION

KW - PHASE-SEPARATION

KW - POLYPEPTIDE-CHAINS

KW - PROTHYMOSIN-ALPHA

KW - SECONDARY STRUCTURE

KW - STABILITY

KW - STATE

KW - TERMINAL DOMAIN

KW - THERMODYNAMIC PARAMETERS

UR - http://www.scopus.com/inward/record.url?scp=85058185957&partnerID=8YFLogxK

UR - http://www.mendeley.com/research/folding-polyamino-acids-intrinsically-disordered-proteins-overcrowded-milieu-induced-ph-change

U2 - 10.1016/j.ijbiomac.2018.12.038

DO - 10.1016/j.ijbiomac.2018.12.038

M3 - Article

VL - 125

SP - 244

EP - 255

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

SN - 0141-8130

ER -