Aggregation properties of a disordered protein are tunable by pH and depend on its net charge per residue - Tedeschi, Giulia; Mangiagalli, Marco; Chmielewska, Sara; Lotti, Marina; Natalello, Antonino; Brocca, Stefania (Biochimica et biophysica acta. General subjects, 2017)
Keywords: amino acid composition; Amino Acid Sequence - genetics; electrostatic interactions; green fluorescent protein; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; hydrophobicity; IDPs; Intrinsically Disordered Proteins - chemistry; Intrinsically Disordered Proteins - genetics; Isoelectric point; Kinetics; Measles morbillivirus; Measles virus - chemistry; Measles virus - genetics; moieties; NCPR; phosphoproteins; Protein Aggregates - genetics; Protein aggregation; Protein Conformation; Protein Folding; Protein solubility; Solubility; Static Electricity; Viral Proteins - chemistry; Viral Proteins - genetics; CD; Protein aggregation; IMAC; Protein solubility; GFP; RC; PB; NCPR; FCR; Isoelectric point; FTIR; PNT; pI; IDPs; ATR