Structural biology can provide three-dimensional structures for proteins of unknown function.
When sequence or structure comparisons fail to suggest a function, insights can come from …

Protein structure prediction from amino acid sequence has been one of the most challenging
aspects in computational structural biology despite significant progress in recent years …

The state-of-the-art to assess the structural quality of docking models is currently based on
three related yet independent quality measures: Fnat, LRMS, and iRMS as proposed and …

We have developed a new scoring function, the template modeling score (TM‐score), to
assess the quality of protein structure templates and predicted full‐length models by …

The ability to separate correct models of protein structures from less correct models is of the
greatest importance for protein structure prediction methods. Several studies have examined …

We develop a new threading algorithm MUSTER by extending the previous sequence
profile–profile alignment method, PPA. It combines various sequence and structure …

Methods to reliably estimate the accuracy of 3D models of proteins are both a fundamental
part of most protein folding pipelines and important for reliable identification of the best …

Most bioinformatics analyses require the assembly of a multiple sequence alignment. It has
long been suspected that structural information can help to improve the quality of these …

During recent years many protein fold recognition methods have been developed, based on
different algorithms and using various kinds of information. To examine the performance of …

In this study we present two methods to predict the local quality of a protein model: ProQres
and ProQprof. ProQres is based on structural features that can be calculated from a model …