scholarly article | Q13442814 |
P356 | DOI | 10.1021/ACS.JPCB.5B11767 |
P698 | PubMed publication ID | 26769494 |
P50 | author | Guangfeng Zhou | Q50911013 |
P2093 | author name string | Vincent A Voelz | |
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Protein conformational plasticity and complex ligand-binding kinetics explored by atomistic simulations and Markov models | Q40776037 | ||
Helicity of short E‐R/K peptides | Q41148281 | ||
Improvements in Markov State Model Construction Reveal Many Non-Native Interactions in the Folding of NTL9. | Q41585818 | ||
Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings | Q41811876 | ||
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Solvent-Exposed Salt Bridges Influence the Kinetics of α-Helix Folding and Unfolding | Q42151733 | ||
A competing salt-bridge suppresses helix formation by the isolated C-peptide carboxylate of ribonuclease A | Q42246039 | ||
Markov models of molecular kinetics: generation and validation | Q43633887 | ||
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Kinetic network models of tryptophan mutations in β-hairpins reveal the importance of non-native interactions. | Q53281393 | ||
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Unfolding and folding internal friction of β-hairpins is smaller than that of α-helices | Q86871707 | ||
P433 | issue | 5 | |
P304 | page(s) | 926-935 | |
P577 | publication date | 2016-02-01 | |
P1433 | published in | Journal of Physical Chemistry B | Q668669 |
P1476 | title | Using Kinetic Network Models To Probe Non-Native Salt-Bridge Effects on α-Helix Folding | |
P478 | volume | 120 |
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Q37188955 | Markov models of the apo-MDM2 lid region reveal diffuse yet two-state binding dynamics and receptor poses for computational docking. |
Q47241787 | Mechanisms of Lipid Scrambling by the G Protein-Coupled Receptor Opsin |
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