Autonomous Sequences in Myoglobin Emerging from X-ray Structure of Holomyoglobin.

ABSTRACT: The proposed continuous folding structure units are fundamental to analyze protein structure. Here, we could elucidate for the first time two types of hydrophobic core networks in apomyoglobin using continuous folding structure units. In myoglobin, two autonomous sequences emerged clearly. We could thus characterize the autonomous sequences using well-defined hydrophobic core networks within respective semifolds. A hydrophobic core is defined as a pair of topology-local hydrophobic amino acids in different folding structures. Hydrophobic core formation is indispensable to stabilize the different folding structures via an efficient hydrophobic interaction. Autonomous sequences in myoglobin encode tertiary structure information for semifolds. These sequences fold autonomously into small sets

SUBMITTER: Narita M 

PROVIDER: S-EPMC6648082 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature