Combining Cryo-EM Density Map and Residue Contact for Protein Secondary Structure Topologies.

ABSTRACT: Although atomic structures have been determined directly from cryo-EM density maps with high resolutions, current structure determination methods for medium resolution (5 to 10 Å) cryo-EM maps are limited by the availability of structure templates. Secondary structure traces are lines detected from a cryo-EM density map for α-helices and β-strands of a protein. A topology of secondary structures defines the mapping between a set of sequence segments and a set of traces of secondary structures in three-dimensional space. In order to enhance accuracy in ranking secondary structure topologies, we explored a method that combines three sources of information: a set of sequence segments in 1D, a set of amino acid contact pairs in 2D, and a set of traces in 3D at the secondary structure level. A

SUBMITTER: Alshammari M 

PROVIDER: S-EPMC8624718 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature