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Updated: Jul 5, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

本質的に無秩序なタンパク質の構成均衡の決定における骨幹溶媒相互作用の役割

Hoang T Tran1, Albert Mao, Rohit V Pappu

  • 1Department of Biomedical Engineering and Center for Computational Biology, Washington University in St. Louis, Campus Box 1097, St. Louis, Missouri 63130, USA.

Journal of the American Chemical Society
|May 17, 2008
PubMed
まとめ

本質的に無秩序なタンパク質 (IDP) は,水中の崩壊した構造を好みます. 分子ダイナミクスシミュレーションにより,ポリグリシンが検出されました.

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

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Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

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Protein Folding

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Entropy and Solvation

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Solvating Effects

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Molecular Chaperones and Protein Folding

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The...