A graph-based algorithm for detecting rigid domains in protein structures.

ABSTRACT:

Background

Conformational transitions are implicated in the biological function of many proteins. Structural changes in proteins can be described approximately as the relative movement of rigid domains against each other. Despite previous efforts, there is a need to develop new domain segmentation algorithms that are capable of analysing the entire structure database efficiently and do not require the choice of protein-dependent tuning parameters such as the number of rigid domains.

Results

We develop a graph-based method for detecting rigid domains in proteins. Structural information from multiple conformational states is represented by a graph whose nodes correspond to amino acids. Graph clustering algorithms allow us to reduce the graph and run the Viterbi algorithm on th

SUBMITTER: Dang TKL 

PROVIDER: S-EPMC7881620 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature