The ankyrin repeat (AR) domain of IκBα consists of a cooperative folding unit of roughly four ARs (AR1-AR4) and of two weakly folded repeats (AR5 and AR6). The kinetic folding mechanism of the cooperative subdomain, IκBα ...

Ab initio peptide folding, and its role in the reductionistic approach towards the understanding of protein folding are discussed from the points of view of past, present and possible future developments. It is believed ...

The small helical protein BBL has been shown to fold and unfold in the absence of a free energy barrier according to a battery of quantitative criteria in equilibrium experiments, including probe-dependent equilibrium ...

We explore the possibility of a deep learning (DL) platform that steers drug design to target proteins by inducing binding-competent conformations. We deal with the fact that target proteins are usually not fixed targets ...

훽-Lactamases (penicillinases) facilitate bacterial resistance to antibiotics and are excellent theoretical and experimental models in protein structure, dynamics and evolution. Bacillus licheniformis exo-small penicillinase ...

Nature employs multiple repeat protein scaffolds in order to promote proteinprotein interactions. In this sense, TPR proteins participate in different natural pathways, especially in diverse processes of eukaryotic cells. ...

Natural protein molecules are exceptional polymers. Encoded in apparently random strings of amino-acids, these objects perform clear physical tasks that are rare to find by simple chance. Accurate folding, specific binding, ...

Protein-protein interactions (PPIs) mediate a variety of cellular processes and form complex networks, where connectivity is achieved owing to the “hub” proteins whose interaction with multiple protein partners is facilitated ...

The concept of quality control of protein folding in the secretory pathway emerged in the late 1970s and early 1980s when it was noticed that not in all cases did insertion of proteins in the endoplasmic reticulum (ER) ...