نتایج جستجو برای: CHARMM

تعداد نتایج: 456  

Journal: :Biophysical journal 2013
Magnus Andersson Jakob P Ulmschneider Martin B Ulmschneider Stephen H White

The distribution of peptide conformations in the membrane interface is central to partitioning energetics. Molecular-dynamics simulations enable characterization of in-membrane structural dynamics. Here, we describe melittin partitioning into dioleoylphosphatidylcholine lipids using CHARMM and OPLS force fields. Although the OPLS simulation failed to reproduce experimental results, the CHARMM s...

2009
MICHAEL F. CROWLEY MARK J. WILLIAMSON ROSS C. WALKER

The similarity of the AMBER force field’s energy functional form with that of the CHARMM force field, gives the potential for direct translation of common bonding and nonbonding terms, along with their parameters, present in CHARMM topology and parameter files, with the intent of evaluation within the AMBER software; specifically the SANDER and PMEMD dynamics engines. To this extent, we have cr...

2014
Antti-Pekka Hynninen Michael F. Crowley

We introduce a new faster molecular dynamics (MD) engine into the CHARMM software package. The new MD engine is faster both in serial (i.e., single CPU core) and parallel execution. Serial performance is approximately two times higher than in the previous version of CHARMM. The newly programmed parallelization method allows the MD engine to parallelize up to hundreds of CPU cores.

Journal: :Journal of computational chemistry 2010
Kenno Vanommeslaeghe Elizabeth Hatcher Chayan Acharya Sibsankar Kundu Shijun Zhong Jihyun Shim Eva Darian Olgun Guvench Pedro E. M. Lopes Igor Vorobyov Alexander D. MacKerell

The widely used CHARMM additive all-atom force field includes parameters for proteins, nucleic acids, lipids, and carbohydrates. In the present article, an extension of the CHARMM force field to drug-like molecules is presented. The resulting CHARMM General Force Field (CGenFF) covers a wide range of chemical groups present in biomolecules and drug-like molecules, including a large number of he...

Journal: :Journal of computational chemistry 2009
Bernard R. Brooks Charles L. Brooks Alexander D. MacKerell Lennart Nilsson Robert J. Petrella Benoît Roux Y. Won G. Archontis Christian Bartels Stefan Boresch Amedeo Caflisch Leo S. D. Caves Qiang Cui Aaron R. Dinner Michael Feig S. Fischer Jiali Gao Milan Hodoscek Wonpil Im Krzysztof Kuczera Themis Lazaridis J. Ma V. Ovchinnikov Emanuele Paci Richard W. Pastor C. B. Post J. Z. Pu Michael Schaefer Bruce Tidor Richard M. Venable H. Lee Woodcock X. Wu W. Yang Darrin M. York Martin Karplus

CHARMM (Chemistry at HARvard Molecular Mechanics) is a highly versatile and widely used molecular simulation program. It has been developed over the last three decades with a primary focus on molecules of biological interest, including proteins, peptides, lipids, nucleic acids, carbohydrates, and small molecule ligands, as they occur in solution, crystals, and membrane environments. For the stu...

Journal: :Journal of Pharmaceutical Negative Results 2023

Breast cancer is one of the most common malignancies among women globally, posing a major public health burden. This study primly aimed to theoretically prove formation silver nanoparticles by Dimocarpus longan fruit phytoconstituents and targeted delivery phytoconstituent inside cavity HER2 protein. The algorithm adsorption location CHARMm-based docking were used find interaction between atoms...

2014
Trang Truc Nguyen Man Hoang Viet Mai Suan Li

The influence of water models SPC, SPC/E, TIP3P, and TIP4P on ligand binding affinity is examined by calculating the binding free energy ΔG(bind) of oseltamivir carboxylate (Tamiflu) to the wild type of glycoprotein neuraminidase from the pandemic A/H5N1 virus. ΔG(bind) is estimated by the Molecular Mechanic-Poisson Boltzmann Surface Area method and all-atom simulations with different combinati...

2002
Michela Taufer Egon Perathoner Andrea Cavalli Amedeo Caflisch Thomas Stricker

The molecular dynamics code CHARMM is a popular research tool for computational biology. An increasing number of researchers are currently looking for affordable and adequate platforms to execute CHARMM or similar codes. To address this need, we analyze the resource requirements of a CHARMM molecular dynamics simulation on PC clusters with a particle mesh Ewald (PME) treatment of longrange elec...

Journal: :Advances in protein chemistry and structural biology 2014
Sunhwan Jo Xi Cheng Shahidul M Islam Lei Huang Huan Rui Allen Zhu Hui Sun Lee Yifei Qi Wei Han Kenno Vanommeslaeghe Alexander D MacKerell Benoît Roux Wonpil Im

CHARMM-GUI, http://www.charmm-gui.org, is a web-based graphical user interface to prepare molecular simulation systems and input files to facilitate the usage of common and advanced simulation techniques. Since it is originally developed in 2006, CHARMM-GUI has been widely adopted for various purposes and now contains a number of different modules designed to setup a broad range of simulations ...

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