6533b836fe1ef96bd12a13c6
RESEARCH PRODUCT
New Insights into Protein (Un)Folding Dynamics.
Patrick SenetPatrick SenetHarold A. ScheragaYoann CoteGia G. MaisuradzePatrice Delaruesubject
Protein FoldingChemistryOpen problemBiophysicsProteinsSequence (biology)Molecular Dynamics SimulationIntrinsically disordered proteinsArticleFolding (chemistry)Intrinsically Disordered ProteinsCrystallographyMolecular dynamicsSide chainBiophysicsHumansThermodynamicsGeneral Materials ScienceProtein foldingAmino Acid SequencePhysical and Theoretical ChemistryPeptidesPeptide sequencedescription
A fundamental open problem in biophysics is how the folded structure of the main chain (MC) of a protein is determined by the physics of the interactions between the side-chains (SCs). All-atom molecular dynamics simulations of a model protein (Trp-cage) revealed that strong correlations between the motions of the SCs and the MC occur transiently at 380 K in unfolded segments of the protein, and during the simulations of the whole amino-acid sequence at 450 K. The high correlation between the SC and MC fluctuations is a fundamental property of the unfolded state and is also relevant to unstructured proteins as Intrinsically Disordered Proteins (IDPs), for which new reaction coordinates are introduced. The presented findings may open a new door as to how functions of IDPs are related to conformations, which play a crucial role in neurodegenerative diseases.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2015-04-14 | The journal of physical chemistry letters |