title: Unfolded in vacuo lysozyme folds into native, quasinative, and compact structures.
abstract: We show that the relaxation dynamics of unfolded in vacuo lysozyme is not random. Analyses of molecular dynamics trajectories in a convenient space of molecular shape descriptors reveal a "favored" pattern of transitions leading to stable conformations. The relaxation paths exhibit a balanced change in shape features: globular spheroids are formed slowly enough to allow the proper entanglement of secondary-structural elements. The present study shows that a protein in vacuo can actually (re)fold into native and quasinative structures. The driving force for these transformations is intrinsic to the polypeptide chain.
authors.affiliation: Département de Chimie et Biochimie, Laurentian University, Sudbury, Ontario, Canada.
authors.forename: G A
authors.initials: GA
authors.lastname: Arteca
authors.forename: I
authors.initials: I
authors.lastname: Velázquez
authors.forename: C T
authors.initials: CT
authors.lastname: Reimann
authors.forename: O
authors.initials: O
authors.lastname: Tapia
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D066298:In Vitro Techniques; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013816:Thermodynamics; D014618:Vacuum
chemical_list: D009113:Muramidase