Current Protein and Peptide Science - Volume 13, Issue 1, 2012

This issue inaugurates volume 13 of Current Protein & Peptide Science. The previous 12 volumes have achieved wide recognition by the protein and peptide research communities, as evidenced by the Impact Factor of 3.83. CPPS now publishes 8 issues per year and we expect that about half of these will be special Hot Topics issues, such as the present one. These issues are organized by a scientist who is a leader in a particular d Read More

INTRODUCTION Recent bioinformatics studies revealed that proteins without stable tertiary and/or secondary structure are very common in nature [1-6]. These highly fluctuable proteins are biologically active yet fail to form specific 3D structures, existing as collapsed or extended dynamic conformational ensembles [3, 7-13]. They constitute an important addition to the protein kingdom [14], which for a long time was consid Read More

Intrinsic disorder is relatively common in proteins, plays important roles in numerous cellular activities, and its prevalence was implicated in various human diseases. However, annotations of the disorder lag behind the rapidly increasing number of known protein chains. The last decade observed development of a relatively large number of in-silico methods that predict the disorder using the protein sequence as their input. We per Read More

During the last decade, network approaches became a powerful tool to describe protein structure and dynamics. Here we review the links between disordered proteins and the associated networks, and describe the consequences of local, mesoscopic and global network disorder on changes in protein structure and dynamics. We introduce a new classification of protein networks into ‘cumulus-type’, i.e., those similar to puffy (wh Read More

Intrinsically unfolded proteins (IUPs) do not obey the golden rule of structural biology, 3D structure = function, as they manifest their inherent functions without resorting to three-dimensional structures. Absence of a compact globular topology in these proteins strongly implies that their ligand recognition processes should involve factors other than spatially well-defined binding pockets. Heteronuclear multidimensional (H Read More

While the crucial role of intrinsically disordered proteins (IDPs) in the cell cycle is now recognized, deciphering their molecular mode of action at the structural level still remains highly challenging and requires a combination of many biophysical approaches. Among them, small angle X-ray scattering (SAXS) has been extremely successful in the last decade and has become an indispensable technique for addressing many of Read More

Small heat shock proteins (sHsp) form a large ubiquitous family of proteins expressed in all phyla of living organisms. The members of this family have low molecular masses (13-43 kDa) and contain a conservative α-crystallin domain. This domain (about 90 residues) consists of several β-strands forming two β-sheets packed in immunoglobulinlike manner. The α-crystallin domain plays an important role in formation of stab Read More

Intrinsically disordered proteins are highly abundant in all kingdoms of life, and several protein functional classes, such as transcription factors, transcriptional regulators, hub and scaffold proteins, signaling proteins, and chaperones are especially enriched in intrinsic disorder. One of the unique cellular reactions to protein damaging stress is the socalled heat shock response that results in the upregulation of heat shock pr Read More