B Toader, FJ Sigworth, RR Lederman - Journal of molecular biology, 2023 - Elsevier
Macromolecules change their shape (conformation) in the process of carrying out their functions. The imaging by cryo-electron microscopy of rapidly-frozen, individual copies of …
Resolving the structural variability of proteins is often key to understanding the structure– function relationship of those macromolecular machines. Single particle analysis using …
Biological macromolecules and assemblies precisely rearrange their atomic 3D structures to execute cellular functions. Understanding the mechanisms by which these molecular …
Single particle cryo-electron microscopy (cryo-EM) has emerged as the prevailing method for near-atomic structure determination, shedding light on the important molecular …
There is a variety of experimental and computational techniques available to explore protein dynamics, each presenting advantages and limitations. One promising experimental …
Cryoelectron microscopy (cryo-EM) methods have made meaningful contributions in a wide variety of scientific research fields. In structural biology, cryo-EM routinely elucidates …
ManifoldEM is an established method of geometric machine learning developed to extract information on conformational motions of molecules from their projections obtained by …
Analyzing dynamical data often requires information of the temporal labels, but such information is unavailable in many applications. Recovery of these temporal labels, closely …
Biomolecules undergo continuous conformational motions, a subset of which are functionally relevant. Understanding, and ultimately controlling biomolecular function are …