Spontaneous refolding of the large multidomain protein malate synthase G proceeds through misfolding traps.

ABSTRACT: Most protein folding studies until now focus on single domain or truncated proteins. Although great insights in the folding of such systems has been accumulated, very little is known regarding the proteins containing multiple domains. It has been shown that the high stability of domains, in conjunction with inter-domain interactions, manifests as a frustrated energy landscape, causing complexity in the global folding pathway. However, multidomain proteins despite containing independently foldable, loosely cooperative sections can fold into native states with amazing speed and accuracy. To understand the complexity in mechanism, studies were conducted previously on the multidomain protein malate synthase G (MSG), an enzyme of the glyoxylate pathway with four distinct and adjacent domains. I

SUBMITTER: Kumar V 

PROVIDER: S-EPMC6109912 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature