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Daniel T. Mainz

Researcher at California Institute of Technology

Publications -  12
Citations -  13251

Daniel T. Mainz is an academic researcher from California Institute of Technology. The author has contributed to research in topics: Ab initio & Chaotropic agent. The author has an hindex of 9, co-authored 12 publications receiving 11162 citations. Previous affiliations of Daniel T. Mainz include D. E. Shaw Research & Schrödinger.

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Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy.

TL;DR: Glide approximates a complete systematic search of the conformational, orientational, and positional space of the docked ligand to find the best docked pose using a model energy function that combines empirical and force-field-based terms.
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Extra Precision Glide: Docking and Scoring Incorporating a Model of Hydrophobic Enclosure for Protein-Ligand Complexes

TL;DR: Enrichment results demonstrate the importance of the novel XP molecular recognition and water scoring in separating active and inactive ligands and avoiding false positives.
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Integrated Modeling Program, Applied Chemical Theory (IMPACT).

TL;DR: An overview of the IMPACT molecular mechanics program is provided with an emphasis on recent developments and a description of its current functionality and a status report for the fixed charge and polarizable force fields is included.
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Parametrizing a polarizable force field from ab initio data. I. The fluctuating point charge model

TL;DR: In this paper, a polarizable force field for peptides was developed using all-atom OPLS (OPLS-AA) nonelectrostatic terms and electrostatics based on a fluctuating charge model and fit to ab initio calculations of polarization responses.
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Stabilization of coiled-coil peptide domains by introduction of trifluoroleucine.

TL;DR: The results suggest that fluorination of hydrophobic substructures in peptides and proteins may provide new means of increasing protein stability, enhancing protein assembly, and strengthening receptor-ligand interactions.