Gfeller, David; Michielin, Olivier; Zoete, Vincent published an article in 2012, the title of the article was Expanding molecular modeling and design tools to non-natural sidechains.Safety of H-Phg(4-OH)-OH And the article contains the following content:
Protein-protein interactions encode the wiring diagram of cellular signaling pathways and their deregulations underlie a variety of diseases, such as cancer. Inhibiting protein-protein interactions with peptide derivatives is a promising way to develop new biol. and therapeutic tools. Here, the authors develop a general framework to computationally handle hundreds of non-natural amino acid sidechains and predict the effect of inserting them into peptides or proteins. The authors first generate all structural files (pdb and mol2), as well as parameters and topologies for standard mol. mechanics software (CHARMM and Gromacs). Accurate predictions of rotamer probabilities are provided using a novel combined knowledge and physics based strategy. Non-natural sidechains are useful to increase peptide ligand binding affinity. The authors’ results obtained on non-natural mutants of a BCL9 peptide targeting beta-catenin show very good correlation between predicted and exptl. binding free-energies, indicating that such predictions can be used to design new inhibitors. Data generated as well as PyMOL and UCSF Chimera plug-ins for user-friendly visualization of non-natural sidechains, are all available at http://www.swisssidechain.ch. The authors’ results enable researchers to rapidly and efficiently work with hundreds of non-natural sidechains. © 2012 Wiley Periodicals, Inc. The experimental process involved the reaction of H-Phg(4-OH)-OH(cas: 32462-30-9).Safety of H-Phg(4-OH)-OH
The Article related to mol model design nonnatural side chain protein peptide interaction, Biochemical Methods: Other (Not Covered At Other Subsections) and other aspects.Safety of H-Phg(4-OH)-OH
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