MolProbity is a structure-validation web service that provides broad-spectrum solidly based
evaluation of model quality at both the global and local levels for both proteins and nucleic …

This paper describes the current update on macromolecular model validation services that
are provided at the MolProbity website, emphasizing changes and additions since the …

What conformations do protein molecules populate in solution? Crystallography provides a
high-resolution description of protein structure in the crystal environment, while NMR …

Many proteins have small-molecule binding pockets that are not easily detectable in the
ligand-free structures. These cryptic sites require a conformational change to become apparent; …

10.7554/eLife.07574.001 Determining the interconverting conformations of dynamic proteins
in atomic detail is a major challenge for structural biology. Conformational heterogeneity in …

Most macromolecular X-ray structures are determined from cryocooled crystals, but it is
unclear whether cryocooling distorts functionally relevant flexibility. Here we compare …

10.7554/eLife.36307.001 Allostery is an inherent feature of proteins, but it remains challenging
to reveal the mechanisms by which allosteric signals propagate. A clearer understanding …

We have developed a suite of protein redesign algorithms that improves realistic in silico
modeling of proteins. These algorithms are based on three characteristics that make them …

Much of our current understanding of how small-molecule ligands interact with proteins stems
from X-ray crystal structures determined at cryogenic (cryo) temperature. For proteins alone…

Computational protein and drug design generally require accurate modeling of protein
conformations. This modeling typically starts with an experimentally determined protein structure …