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Atomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein

  • 2019-12
  • Lee, Ju Hwan. (2019-12). Atomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein. doi: 10.1038/s41598-019-55661-2
  • Nature Research
  • View : 720
  • Download : 181

Sibe: A computation tool to apply protein sequence statistics to predict folding and design in silico

  • 2019-09
  • Cheung, Ngaam J. (2019-09). Sibe: A computation tool to apply protein sequence statistics to predict folding and design in silico. doi: 10.1186/s12859-019-2984-1
  • BioMed Central Ltd.
  • View : 645
  • Download : 144

De novo protein structure prediction using ultra-fast molecular dynamics simulation

  • 2018-11
  • Cheung, J. Ngaam. (2018-11). De novo protein structure prediction using ultra-fast molecular dynamics simulation. doi: 10.1371/journal.pone.0205819
  • Public Library of Science
  • View : 738
  • Download : 105

Exploring the Ligand Efficacy of Cannabinoid Receptor 1 (CB1) using Molecular Dynamics Simulations

  • 2018-09
  • Jung, Sang Won. (2018-09). Exploring the Ligand Efficacy of Cannabinoid Receptor 1 (CB1) using Molecular Dynamics Simulations. Scientific Reports, 8(1), 171–172. doi: 10.1038/s41598-018-31749-z
  • Nature Publishing Group
  • View : 655
  • Download : 138
  • Skinner, John J.
  • Yu, Wookyung
  • Gichana, Elizabeth K.
  • Baxa, Michael C.
  • Hinshaw, James R.
  • Freed, Karl F.
  • Sosnick, Tobin R.
  • 2014-11-11
  • Skinner, John J. (2014-11-11). Benchmarking all-atom simulations using hydrogen exchange. Proceedings of the National Academy of Sciences of the United States of America, 111(45), 15975–15980. doi: 10.1073/pnas.1404213111
  • National Academy of Sciences
  • View : 950
  • Download : 0
  • Baxa, Michael C.
  • Yu, Wookyung
  • Adhikari, Aashish N.
  • Ge, Liang
  • Xia, Zhen
  • Zhou, Ruhong
  • Freed, Karl F.
  • Sosnick, Tobin R.
  • 2015-07-07
  • Baxa, Michael C. (2015-07-07). Even with nonnative interactions, the updated folding transition states of the homologs Proteins G & L are extensive and similar. Proceedings of the National Academy of Sciences of the United States of America, 112(27), 8302–8307. doi: 10.1073/pnas.1503613112
  • National Academy of Sciences
  • View : 1295
  • Download : 0
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