We describe a new approach, based on the energy of non-local interactions, to assess
protein structures. The method uses a very sensitive and accurate atomic mean force …

Abstract ANOLEA (Atomic Non-Local Environment Assessment) is a www server that
performs energy calculations at the atomic level in protein structures. The calculations …

We present an approach that is able to detect native folds amongst a large number of non-
native conformations. The method is based on the compilation of potentials of mean force of …

The structural stability of a protein requires a large number of interresidue interactions. The
energetic contribution of these can be approximated by low-resolution force fields extracted …

A protein structure model generally needs to be evaluated to assess whether or not it has
the correct fold. To improve fold assessment, four types of a residue‐level statistical potential …

The size of the protein database (PDB) makes it now feasible to arrive at statistical
conclusions regarding structural effects of crystal packing. These effects are relevant for …

Important properties of globular proteins, such as the stability of the folded state, depend
sensitively on interactions with solvent molecules. An excluded volume approximation to …

An approach based exclusively on finding the global minimum of an appropriate potential
energy function has been used to predict the unknown structures of five globular proteins …

Today's energy functions are not able yet to distinguish reliably between correct and almost
correct protein models. Improving these near‐native models is currently a major bottle‐neck …

Standard ranges of atomic and residue volumes are computed in 64 highly resolved and
well-refined protein crystal structures using the classical Voronoi procedure. Deviations of …