title: New Insights into Protein (Un)Folding Dynamics.
abstract: 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.
authors: Yoann
authors: Y
authors: Cote
authors: Gia G
authors: GG
authors: Maisuradze
authors: Patrice
authors: P
authors: Delarue
authors: Harold A
authors: HA
authors: Scheraga
authors: Patrick
authors: P
authors: Senet
mesh_terms: D000595:Amino Acid Sequence; D001703:Biophysics; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry; D056004:Molecular Dynamics Simulation; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D064267:Intrinsically Disordered Proteins; D010455:Peptides; D011506:Proteins; C508725:Trp-cage peptide