Elucidating structural variability in p53 conformers using combinatorial refinement strategies and molecular dynamics.

ABSTRACT: Low molecular weight proteins and protein assemblies can now be investigated using cryo-electron microscopy (EM) as a complement to traditional structural biology techniques. It is important, however, to not lose sight of the dynamic information inherent in macromolecules that give rise to their exquisite functionality. As computational methods continue to advance the field of biomedical imaging, so must strategies to resolve the minute details of disease-related entities. Here, we employed combinatorial modeling approaches to assess flexible properties among low molecular weight proteins (~100 kDa or less). Through a blend of rigid body refinement and simulated annealing, we determined new hidden conformations for wild type p53 monomer and dimer forms. Structures for both states converged

SUBMITTER: Parves MR 

PROVIDER: S-EPMC10732606 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature