Ontology highlight
ABSTRACT:
SUBMITTER: Xu D
PROVIDER: S-EPMC9059239 | biostudies-literature | 2021 Aug
REPOSITORIES: biostudies-literature
Xu Da D Meisburger Steve P SP Ando Nozomi N
Biochemistry 20210722 30
Correlated motions in proteins arising from the collective movements of residues have long been proposed to be fundamentally important to key properties of proteins, from allostery and catalysis to evolvability. Recent breakthroughs in structural biology have made it possible to capture proteins undergoing complex conformational changes, yet intrinsic correlated motions within a conformation remain one of the least understood facets of protein structure. For many decades, the analysis of total X ...[more]