Dynamics of lysozyme structure network: probing the process of unfolding.

ABSTRACT: Recently we showed that the three-dimensional structure of proteins can be investigated from a network perspective, where the amino acid residues represent the nodes in the network and the noncovalent interactions between them are considered for the edge formation. In this study, the dynamical behavior of such networks is examined by considering the example of T4 lysozyme. The equilibrium dynamics and the process of unfolding are followed by simulating the protein at 300 K and at higher temperatures (400 K and 500 K), respectively. The snapshots of the protein structure from the simulations are represented as protein structure networks in which the strength of the noncovalent interactions is considered an important criterion in the construction of edges. The profiles of the network paramet

SUBMITTER: Ghosh A 

PROVIDER: S-EPMC1864820 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature