Abstract
Internal ionizable residues in proteins have shifted apparent pKa values with respect their intrinsic pKa in bulk water. To understand the atomistic mechanism responsible for this shift in pKa, we study the pH-dependent conformational changes in mutants of Staphylococcal Nuclease (SNase) having single internal ionizable residues. We used pH Replica Exchange Molecular Dynamics (pH-REMD) for our calculations. We present thermodynamic models to find the ‘conformation-specific pKa values’ of the internal ionizable residues and explain their association with the observed ‘apparent pKa’. Further, we study the pH-dependent structural and thermodynamic properties of ionizable residue pairs within the hydrophobic interior of SNase.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.