Explaining Conformational Diversity in Protein Families through Molecular Motions.
Ontology highlight
ABSTRACT: Proteins play a central role in biological processes, and understanding their conformational variability is crucial for unraveling their functional mechanisms. Recent advancements in high-throughput technologies have enhanced our knowledge of protein structures, yet predicting their multiple conformational states and motions remains challenging. This study introduces Dimensionality Analysis for protein Conformational Exploration (DANCE) for a systematic and comprehensive description of protein families conformational variability. DANCE accommodates both experimental and predicted structures. It is suitable for analysing anything from single proteins to superfamilies. Employing it, we clustered all experimentally resolved protein structures available in the Protein Data Bank into conformati
SUBMITTER: Lombard V
PROVIDER: S-EPMC11237097 | biostudies-literature | 2024 Jul
REPOSITORIES: biostudies-literature
ACCESS DATA