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Tom Kurtzman

Publications and source records attributed to Tom Kurtzman.

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Solv-eze: Automated Placement of Explicit Water Molecules Using 3D-RISM

Molecular dynamics (MD) simulations are widely used to study biological systems, where water molecules often play a critical role in protein-ligand interactions. In conventional MD preparation protocols, water molecules are typically added from a pre-equilibrated solvent box and removed using conservative steric cutoffs, an approach that can eliminate important interfacial waters that are often not recovered during equilibration due to kinetic barriers limiting exchange with bulk solvent. In this work, we present an automated and computationally efficient method for placing water molecules around biomolecular solutes using three-dimensional reference interaction site model (3D-RISM) solvent density distributions. By identifying regions of high solvent probability, the method generates physically meaningful initial hydration structures without requiring extended sampling or specialized techniques such as grand canonical Monte Carlo (MC) or hybrid MC/MD approaches, and will be released as an update to AmberTools 26, enabling seamless integration into standard MD preparation pipelines. We validated the approach on a diverse set of protein-ligand complexes with crystallographically resolved bridging waters, showing that the method reproduced over 80% of experimentally observed bridging waters and 85% of buried waters not accessible to the bulk. Subsequent energy minimization of both crystallographic and predicted waters further improved agreement. Overall, this method enables more accurate and practical initialization of interfacial hydration, improving the reliability of MD simulations with modest computational cost relative to routine system preparation.

physics.chem-ph

Application of the Alchemical Transfer and Potential of Mean Force Methods to the SAMPL8 Host-Guest Blinded Challenge

We report the results of our participation in the SAMPL8 GDCC Blind Challenge for host-guest binding affinity predictions. Absolute binding affinity prediction is of central importance to the biophysics of molecular association and pharmaceutical discovery. The blinded SAMPL series have provided an important forum for assessing the reliability of binding free energy methods in an objective way. In this blinded challenge, we employed two binding free energy methods, the newly developed alchemical transfer method (ATM) and the well-established potential of mean force (PMF) physical pathway method, using the same setup and force field model. The calculated binding free energies from the two methods are in excellent quantitative agreement. Importantly, the results from the two methods were also found to agree well with the experimental binding affinities released subsequently, with an $R^2$ of 0.89 (ATM) and 0.83 (PMF). Given that the two free energy methods are based on entirely different thermodynamic pathways, the close agreement between the results from the two methods and their general agreement with the experimental binding free energies are a testament to the high quality achieved by theory and methods. The study provides further validation of the novel ATM binding free energy estimation protocol and it paves the way to further extensions of the method to more complex systems.

physics.chem-ph

Inclusion of Enclosed Hydration Effects in the Binding Free Energy Estimation of Dopamine D3 Receptor Complexes

Confined hydration and conformational flexibility are some of the challenges encountered for the rational design of selective antagonists of G-protein coupled receptors. We present a set of C3-substituted (-)-stepholidine derivatives as potent binders of the dopamine D3 receptor. The compounds are characterized biochemically, as well as by computer modeling using a novel molecular dynamics-based alchemical binding free energy approach which incorporates the effect of the displacement of enclosed water molecules from the binding site. The free energy of displacement of specific hydration sites is obtained using the Hydration Site Analysis method with explicit solvation. This work underscores the critical role of confined hydration and conformational reorganization in the molecular recognition mechanism of dopamine receptors and illustrates the potential of binding free energy models to represent these key phenomena.

physics.bio-ph