Cooperativity and Folding Kinetics in a Multidomain Protein with Interwoven Chain Topology.

ABSTRACT: Although a large percentage of eukaryotic proteomes consist of proteins with multiple domains, not much is known about their assembly mechanism, especially those with intricate native state architectures. Some have a complex topology in which the structural elements along the sequence are interwoven in such a manner that the domains cannot be separated by cutting at any location along the sequence. Such proteins are multiply connected multidomain proteins (MMPs) with the three-domain (NMP, LID, and CORE) phosphotransferase enzyme adenylate kinase (ADK) being an example. We devised a coarse-grained model to simulate ADK folding initiated by changing either the temperature or guanidinium chloride (GdmCl) concentration. The simulations reproduce the experimentally measured melting temperature

SUBMITTER: Liu Z 

PROVIDER: S-EPMC9228575 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature