Publications by authors named "Aaron J Adkins"
Article Synopsis
- Charged residues on proteins are essential for stability and binding, but high net-charge regions can destabilize proteins while helping them interact with oppositely charged targets.
- Researchers studied the folding of a specific yeast protein domain (SH3) and found that increased salt concentrations surprisingly stabilize its structure by mimicking interactions that occur during target binding.
- The study revealed that while the protein experiences both hydrophobic collapse and electrostatic repulsion during folding, the formation of favorable interactions like salt-bridges and hydrogen bonds allows it to maintain a functional, folded state after overcoming initial challenges.
Article Synopsis
- Charged residues on proteins are crucial for stability and interactions, often creating regions that might destabilize proteins but are necessary for binding to oppositely charged targets.
- The study found that increasing salt concentrations stabilizes the folding of the yeast SH3 domain by reducing electrostatic repulsion, thanks to effects like Debye-Huckel screening.
- Experiments revealed that while the addition of urea or salt affects folding rates, the key folding events happen in the transition state, allowing the protein domain to efficiently fold and prepare for binding despite its high charge.
