The biophysical principles that modulate protein folding landscape are still an extremely active field of research with great debate around the folding pathway.

 

While many (if not most) biological roles are credited to properly folded proteins, unfolded states, intrinsically disordered regions (IDRs) or entire intrinsically disordered proteins (IDPs) also play vital roles in numerous diseases (e.g.: neurodegenerative diseases) and cellular processes (e.g.: regulation of transcription and translation, signal transduction, phosphorylation or storage of small molecules).

 

Despite their apparent simplicity (in the sense that they lack the organisation and complexity of ordered proteins), due to their dynamic ensemble nature and a scarcity of experimental restraints and reduced informational content of their amino acid sequences, disordered states of proteins are difficult to characterise structurally. Yet, despite these caveats, IDPs may not be completely random entities, since they evolved to have some adjustable, controllable, regulable, tuneable, and, oftentimes, very specific properties required for their biological functions.

 

| The optimisation of solvent environment envisaging the tuning of protein folding landscape can be done with ionic liquids (ILs).

 

 

Ionic liquids (ILs) are organic salts, composed entirely by positive and negative ions, with low melting points (typically below 100 °C) and their bulk and interfacial behaviour is complex, governed by Coulombic, van der Waals, dipole-dipole, hydrogen-bonding, and solvophobic forces. Advantageous characteristics of ionic liquids are their low melting temperatures, low flammability, low volatilities and relatively low cost. Due to their tuneable physical properties ILs can be adjusted to different experimental requirements spanning from protein extraction to enzyme catalysis at elevated temperature. Because of this, ILs are frequently designated as “designer solvents”.

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Using Nuclear Magnetic Resonance (NMR) spectroscopy, we explore the stabilisation, interaction, structural, kinetic and thermodynamic changes of proteins in the presence of different ionic liquids.

 

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