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Unfolded in vacuo lysozyme folds into native, quasinative, and compact structures
G A Arteca1, I Velázquez, C T Reimann
1Département de Chimie et Biochimie, Laurentian University, Sudbury, Ontario, Canada.
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.
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