Results 141 to 150 of about 6,457,465 (175)
Some of the next articles are maybe not open access.
Nanoscale, 2019
Nanopore based sensors constitute a promising approach to single molecule protein characterization being able, in principle, to detect sequences, structural elements and folding states of proteins and polypeptide chains.
Emma Letizia Bonome +2 more
semanticscholar +1 more source
Nanopore based sensors constitute a promising approach to single molecule protein characterization being able, in principle, to detect sequences, structural elements and folding states of proteins and polypeptide chains.
Emma Letizia Bonome +2 more
semanticscholar +1 more source
Hemolysins: Pore-forming proteins in invertebrates
Experientia, 1990Invertebrates possess lytic molecules which lyse vertebrate erythrocytes. In all the species studied so far, hemolytic activity depends on proteins which possess a wide range of reactivity. It is generally calcium-dependent and heat-labile, although calcium-independent and heat-stable hemolysins have also been detected.
openaire +2 more sources
Unfolding and Translocation of Proteins Through an Alpha-Hemolysin Nanopore by ClpXP
2020Proteins present a significant challenge for nanopore-based sequence analysis. This is partly due to their stable tertiary structures that must be unfolded for linear translocation, and the absence of regular charge density. To address these challenges, here we describe how ClpXP, an ATP-dependent protein unfoldase, can be harnessed to unfold and ...
Jeff, Nivala +4 more
openaire +2 more sources
All-Atom Molecular Dynamics Simulation of Protein Translocation through an α-Hemolysin Nanopore
The Journal of Physical Chemistry Letters, 2015Nanopore sensing is attracting the attention of a large and varied scientific community. One of the main issues in nanopore sensing is how to associate the measured current signals to specific features of the molecule under investigation. This is particularly relevant when the translocating molecule is a protein and the pore is sufficiently narrow to ...
Di Marino, Daniele +3 more
openaire +4 more sources
Thermodynamics of a Protein Acylation: Activation of Escherichia coli Hemolysin Toxin
Biochemistry, 2004HlyC, hemolysin-activating lysine-acyltransferase, catalyses the acylation (from acyl-acyl carrier protein [ACP]) of Escherichia coli prohemolysin (proHlyA) on the epsilon-amino groups of specific lysine residues, 564 and 690 of the 1024 amino acid primary structure, to form hemolysin (HlyA).
Worsham, Lesa M.S. +2 more
openaire +3 more sources
Molecular and General Genetics MGG, 1994
Secretion of Escherichia coli hemolysin is mediated by a sec-independent pathway which requires the products of at least three genes, hlyB, hlyD and tolC. Two regions of HlyD were studied. The first region (region A), consisting of the 33-amino acid, C-terminal part of the HlyD protein, is predicted to form a potential helix-loop-helix structure.
R, Schülein +4 more
openaire +2 more sources
Secretion of Escherichia coli hemolysin is mediated by a sec-independent pathway which requires the products of at least three genes, hlyB, hlyD and tolC. Two regions of HlyD were studied. The first region (region A), consisting of the 33-amino acid, C-terminal part of the HlyD protein, is predicted to form a potential helix-loop-helix structure.
R, Schülein +4 more
openaire +2 more sources
[4] Membrane protein crystallization: Application of sparse matrices to the α-hemolysin heptamer
1997Publisher Summary The three-dimensional crystals of membrane proteins can be divided into two classes: (1) type I crystals, which consist of layers of molecules in which the hydrophobic contacts between the lipid-embedded portions of a protein mediate the intralayer interactions and the hydrophilic contacts between the domains exposed to aqueous ...
Langzhou, Song, J Eric, Gouaux
openaire +2 more sources
Translocation Dynamics of Poly(styrenesulfonic acid) through an α-Hemolysin Protein Nanopore
Macromolecules, 2010The transport of linear anionic poly(styrenesulfonic acid) (PSS) chains through an α-hemolysin protein channel, embedded in a lipid bilayer which is suspended on a glass nanopore membrane, is repor...
Qianjin Chen +4 more
openaire +1 more source
Journal of Molecular Graphics and Modelling
Staphylococcus aureus is a common bacterium that causes a variety of infections in humans. This microorganism produces several virulence factors, including hemolysins, which contribute to its disease-causing ability. The treatment of S. aureus infections typically involves the use of antibiotics.
Lennin Isaac Garrido-Palazuelos +8 more
openaire +2 more sources
Staphylococcus aureus is a common bacterium that causes a variety of infections in humans. This microorganism produces several virulence factors, including hemolysins, which contribute to its disease-causing ability. The treatment of S. aureus infections typically involves the use of antibiotics.
Lennin Isaac Garrido-Palazuelos +8 more
openaire +2 more sources