Protein and Peptide Letters - Volume 21, Issue 3, 2014

Most proteinaceous pores are characterized as ionic channels. However, some are also involved in protein translocation through phospholipidic membranes. This concept has evolved slowly in cell biology and in biophysics, requiring the development of adapted electrical and biochemical methods. Protein translocation in mitochondria biogenesis, secretion by endoplasmic reticulum or bacteria, and bacterial toxins internali Read More

When macromolecules such as proteins are forced to translocate through a narrow pore, their conformational entropy is reduced, resulting in a free energy barrier. This free energy barrier is additionally modulated by protein-pore interactions. Furthermore, the driving force of the translocation such as the electrochemical potential gradient and electroosmotic flow navigates the transport of the protein through the f Read More

Biological processes such as protein degradation and mitochondrial protein import require protein passage, or translocation, across narrow pores. In addition to its biological significance, protein translocation through biological or engineered nanopores offers a powerful analytic tool for biophysics and nanotechnology. This mini-review discusses the physical mechanisms of protein translocation, as revealed by computatio Read More

We survey the transport of proteins across nanopores in the framework of coarse-grained modeling. The advantage of a reduced complexity with respect to full-atomistic techniques lies in the possibility of massive sampling of events, thus allowing a statistical mechanical description of translocation in terms of ensemble averages. Often, protein transport through narrow channels tightly couples with unfolding pathways Read More

Recent studies in the area of single-molecule detection of proteins with nanopores show a great promise in fundamental science, bionanotechnology and proteomics. In this mini-review, I discuss a comprehensive array of examinations of protein detection and characterization using protein and solid-state nanopores. These investigations demonstrate the power of the single-molecule nanopore measurements to Read More

In this minireview, the nanopore analysis of peptides and proteins in the presence of divalent metal ions will be surveyed. In all cases the binding of the metal ions causes the peptide or protein to adopt a more compact conformation which can no longer enter the α-hemolysin pore. In the absence of Zn(II) the 30-amino acid Zn-finger peptide can readily translocate the pore; but upon addition of Zn(II) the peptide folds and Read More

In this work, we review the process of protein unfolding characterized by a solid-state nanopore based device. The occupied or excluded volume of a protein molecule in a nanopore depends on the protein’s conformation or shape. A folded protein has a larger excluded volume in a nanopore thus it blocks more ionic current flow than its unfolded form and produces a greater current blockage amplitude. The time duration a pr Read More

In this mini-review we introduce and discuss a new method, at single molecule level, to study the protein folding and protein stability, with a nanopore coupled to an electric detection. Proteins unfolded or partially folded passing through one channel submitted to an electric field, in the presence of salt solution, induce different detectable blockades of ionic current. Their duration depends on protein conformation. For dif Read More

In order to predict enzyme subclasses, this paper builds a new enzyme database in term of previous ideas and methods. Based on protein sequence, by selecting increment of diversity value, low-frequency of power spectral density, matrix scoring values and motif frequency as characteristic parameters to describe the sequence information, a Random Forest algorithm for predicting enzyme subclass is proposed Read More

Ribosome recycling factor (RRF) and elongation factor-G catalyze disassembly of the post-termination complex and recycling of the ribosomal subunits back to a new round of initiation. Thermoanaerobacter tengcongensis survive high temperatures that Escherichia coli cannot, partly due to the higher thermal stability of T. tengcongensis ribosome recycling factor (tteRRF). Here we compared the structural stability of tteRRF a Read More

Leucine rich repeats (LRRs) are present in over 20,000 proteins from viruses to eukaryotes. Two to sixty-two LRRs occur in tandem. Each repeat is typically 20-30 residues long and can be divided into an HCS (Highly conserved segment) and a VS (Variable segment). The HCS part consists of an eleven or a twelve residue stretch, LxxLxLxxNx(x/- )L, in which “L” is Leu, Ile, Val, or Phe, “N” is Asn, Thr, Ser, or Cys, “x” is a non-conserv Read More

KGF (Keratinocyte Growth Factor), also known as FGF7, is a potent mitogen for different types of epithelial cells, which regulates migration and differentiation of these cells and protects them from various insults under stress conditions. KGF is produced by mesenchymal cells and exerts its biological effects via binding to its high-affinity receptor, a splice variant of FGF receptor 2 (FGFR2-IIIb), which is expressed by various ty Read More