RETRACTED: Delineating Conformational Variability in Small Protein Structures Using Combinatorial Refinement Strategies

ABSTRACT: As small protein assemblies and even small proteins are becoming more amenable to cryo-Electron Microscopy (EM) structural studies, it is important to consider the complementary dynamic information present in the data. Current computational strategies are limited in their ability to resolve minute differences among low molecular weight entities. Here, we demonstrate a new combinatorial approach to delineate flexible conformations among small proteins using real-space refinement applications. We performed a meta-analysis of structural data for the SARS CoV-2 Nucleocapsid (N) protein using a combination of rigid-body refinement and simulated annealing methods. For the N protein monomer, we determined three new flexible conformers with good stereochemistry and quantitative comparisons provide

SUBMITTER: Kelly DF 

PROVIDER: S-EPMC10609307 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature