[X] Close
You are about to erase all the values you have customized, search history, page format, etc.
Click here to RESET all values       Click here to GO BACK without resetting any value
Item 1 of about 1
1. Ben-Shimon A, Shalev DE, Niv MY: Protonation States in molecular dynamics simulations of peptide folding and binding. Curr Pharm Des; 2013;19(23):4173-81

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Protonation States in molecular dynamics simulations of peptide folding and binding.
  • Peptides are important signaling modules, acting both as individual hormones and as parts of larger molecules, mediating their protein-protein interactions.
  • Many peptidic and peptidomimetic drugs have reached the marketplace and opportunities for peptide-based drug discovery are on the rise. pH-dependent behavior of peptides is well documented in the context of misfolding diseases and peptide translocation.
  • Changes in the protonation states of peptide residues often have a crucial effect on a peptide's structure, dynamics and function, which may be exploited for biotechnological applications.
  • The current review surveys the increasing levels of sophistication in the treatment of protonation states in computational studies involving peptides.
  • Specifically we describe I) the common practice of assigning a single protonation state and using it throughout the dynamic simulation, II) approaches that consider multiple protonation states and compare computed observables to experimental ones, III) constant pH molecular dynamics methods that couple changes in protonation states with conformational dynamics "on the fly".
  • Applications of conformational dynamics treatment of peptides in the context of binding, folding and interactions with the membrane are presented, illustrating the growing body of work in this field and highlighting the importance of careful handling of protonation states of peptidic residues.
  • [MeSH-major] Molecular Dynamics Simulation. Peptides / chemistry. Protein Folding. Proteins / chemistry. Protons
  • [MeSH-minor] Peptidomimetics. Protein Binding

  • [Email] Email this result item
    Email the results to the following email address:   [X] Close
  • (PMID = 23170889.001).
  • [ISSN] 1873-4286
  • [Journal-full-title] Current pharmaceutical design
  • [ISO-abbreviation] Curr. Pharm. Des.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't; Review
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Peptides; 0 / Peptidomimetics; 0 / Proteins; 0 / Protons
  •  go-up   go-down


Advertisement





Advertisement