The process of heme binding to a protein is prevalent in almost all forms of life to control
many important biological properties, such as O 2-binding, electron transfer, gas sensing or …

Background Accurate prediction of binding residues involved in the interactions between
proteins and small ligands is one of the major challenges in structural bioinformatics. Heme …

Background Heme is an essential molecule and plays vital roles in many biological
processes. The structural determination of a large number of heme proteins has made it …

Background The notion of heme as a regulator of many physiological processes via
transient binding to proteins is one that is recently being acknowledged. The broad spectrum …

Deviant levels of available heme and related molecules can result from pathological
situations such as impaired heme biosynthesis or increased hemolysis as a consequence of …

Abstract Background Heme binding proteins (HBPs) are metalloproteins that contain a heme
ligand (an iron-porphyrin complex) as the prosthetic group. Several computational methods …

Computational identification of heme-binding residues is beneficial for predicting and
designing novel heme proteins. Here we proposed a novel method for heme-binding …

The characteristics of heme prosthetic groups and their binding sites have been analyzed in
detail in a data set of nonhomologous heme proteins. Variations in the shape, volume, and …

Hemes are often incorporated into designed proteins. The importance of the heme ligand
type and its orientation is still a matter of debate. Here, heme ligands and ligand orientation …

Objective: Heme cofactors are essential molecule found in almost all forms of life. Biological
systems depend on heme-protein interactions to carry out basic functions required for their …