Emotional Design. Why We Lo ve (or Hate) Everyday Things. Norman, D. A Volume 2 , Basic Books, 2005. ISSN: 00157120 Publication Title: Basic Books _eprint: arXiv:1011.1669v3doi abstract bibtex Predicting the binding mode of flexible polypeptides to proteins is an important task that falls outside the domain of applicability of most small molecule and protein−protein docking tools. Here, we test the small molecule flexible ligand docking program Glide on a set of 19 non-α-helical peptides and systematically improve pose prediction accuracy by enhancing Glide sampling for flexible polypeptides. In addition, scoring of the poses was improved by post-processing with physics-based implicit solvent MM- GBSA calculations. Using the best RMSD among the top 10 scoring poses as a metric, the success rate (RMSD ≤ 2.0 \AA for the interface backbone atoms) increased from 21% with default Glide SP settings to 58% with the enhanced peptide sampling and scoring protocol in the case of redocking to the native protein structure. This approaches the accuracy of the recently developed Rosetta FlexPepDock method (63% success for these 19 peptides) while being over 100 times faster. Cross-docking was performed for a subset of cases where an unbound receptor structure was available, and in that case, 40% of peptides were docked successfully. We analyze the results and find that the optimized polypeptide protocol is most accurate for extended peptides of limited size and number of formal charges, defining a domain of applicability for this approach.
@book{norman_emotional_2005,
title = {Emotional {Design}. {Why} {We} {Lo} ve (or {Hate}) {Everyday} {Things}},
volume = {2},
isbn = {978-85-7811-079-6},
abstract = {Predicting the binding mode of flexible polypeptides to proteins is an important task that falls outside the domain of applicability of most small molecule and protein−protein docking tools. Here, we test the small molecule flexible ligand docking program Glide on a set of 19 non-α-helical peptides and systematically improve pose prediction accuracy by enhancing Glide sampling for flexible polypeptides. In addition, scoring of the poses was improved by post-processing with physics-based implicit solvent MM- GBSA calculations. Using the best RMSD among the top 10 scoring poses as a metric, the success rate (RMSD ≤ 2.0 {\textbackslash}AA for the interface backbone atoms) increased from 21\% with default Glide SP settings to 58\% with the enhanced peptide sampling and scoring protocol in the case of redocking to the native protein structure. This approaches the accuracy of the recently developed Rosetta FlexPepDock method (63\% success for these 19 peptides) while being over 100 times faster. Cross-docking was performed for a subset of cases where an unbound receptor structure was available, and in that case, 40\% of peptides were docked successfully. We analyze the results and find that the optimized polypeptide protocol is most accurate for extended peptides of limited size and number of formal charges, defining a domain of applicability for this approach.},
publisher = {Basic Books},
author = {Norman, Donald A},
year = {2005},
doi = {10.1017/CBO9781107415324.004},
pmid = {25246403},
note = {ISSN: 00157120
Publication Title: Basic Books
\_eprint: arXiv:1011.1669v3},
keywords = {Diseño Emocional, Evaluación},
}
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