Transcriptional activation domains achieve rapid, dynamic, specific interaction with Mediator through binding of an unstructured peptide to multiple hydrophobic surfaces without particular amino acid side chain interactions.
Quantitative 3D lattice light sheet microscopy of unperturbed cells combined with electron tomography and acute loss of function experiments reveals how dynamic ESCRT-III/Vps4 assemblies succeed in reverse membrane budding on endosomes.
Single-molecule resolution of cAMP binding to the ligand binding domain of pacemaking channels in zero-mode waveguides reveals the dynamics of the distinct steps underlying both binding and isomerization of the binding domain.
A combination of molecular dynamics simulations and X-ray diffraction data has been used to construct more realistic models of proteins and to provide new insights into their interactions with other proteins and biomolecules.
A general machine learning scheme for integrating time-series data from single-molecule experiments and molecular dynamics simulations is proposed and successfully demonstrated for the folding dynamics of the WW domain.
A combination of X-ray crystallography, molecular dynamics and small angle X-ray scattering shows that the transcription antiterminator M2-1 is a structurally dynamic homotetramer that undergoes large concerted conformational changes upon binding its target RNA.