A5063194678- Lipid Membrane Structure and Behavior
- Protein Structure and Dynamics
- Bacterial Genetics and Biotechnology
- RNA and protein synthesis mechanisms
- Escherichia coli research studies
- Virus-based gene therapy research
- Photoreceptor and optogenetics research
- Photosynthetic Processes and Mechanisms
- Spectroscopy and Quantum Chemical Studies
- Cellular transport and secretion
- Clostridium difficile and Clostridium perfringens research
- Receptor Mechanisms and Signaling
- Monoclonal and Polyclonal Antibodies Research
- Neuropeptides and Animal Physiology
- DNA and Nucleic Acid Chemistry
- Hemoglobin structure and function
- Viral gastroenteritis research and epidemiology
- Nanopore and Nanochannel Transport Studies
- Mitochondrial Function and Pathology
- RNA modifications and cancer
- Bee Products Chemical Analysis
- Advanced Biosensing Techniques and Applications
- Gastrointestinal motility and disorders
- Food Chemistry and Fat Analysis
- Parvovirus B19 Infection Studies
University of Kassel
2013-2023
University of Konstanz
2005-2022
Centro de Investigaciones Energéticas, Medioambientales y Tecnológicas
2012
Centre National de la Recherche Scientifique
2006-2011
Institut de Biologie Physico-Chimique
2006-2011
Heidelberg University
2002-2010
German Cancer Research Center
2010
Biologie du Chloroplaste et Perception de la Lumière chez les Microalgues
2006
Sorbonne Université
2006
University of Virginia
1996-2002
Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep integral membrane proteins (MPs) water soluble. In this review, we discuss their structure and solution behavior; the way they associate with MPs; structure, dynamics, properties of resulting complexes. All MPs tested date form water-soluble complexes APols, biochemical stability is in general greatly improved compared detergent solutions. The functionality ligand-binding APol-trapped reviewed,...
We have studied the folding pathway of a β-barrel membrane protein using outer A (OmpA) of<i>Escherichia coli</i> as an example. The deletion gene periplasmic Skp impairs assembly proteins bacteria. investigated how facilitates insertion and completely unfolded OmpA into phospholipid membranes which are biochemical biophysical requirements possible Skp-assisted pathway. In refolding experiments, alone was not sufficient to facilitate OmpA. addition, lipopolysaccharide (LPS) required....
The mechanism of folding and membrane insertion integral proteins, including helix bundle β-barrel proteins is not well understood. A key question whether are coupled or separable processes. We have used the outer protein (OmpA) Escherichia coli as a model to study kinetics into dioleoylphosphatidylcholine (DOPC) bilayers function temperature by gel electrophoresis, protease digestion, fluorescence spectroscopy. OmpA was unfolded in 8 M urea solution (without detergent), refolding initiated...
Unfolded outer membrane protein A (OmpA) of Escherichia coli spontaneously inserts and refolds into lipid bilayers upon dilution denaturing urea. In the accompanying paper, we have developed a new technique, time-resolved distance determination by fluorescence quenching (TDFQ), which is capable monitoring translocation across reporter groups such as tryptophan in real time [Kleinschmidt, J. H., Tamm, L. K. (1999) Biochemistry 38, 4996−5005]. Specifically, shown that wild-type OmpA, contains...
Abstract Outer membrane protein A (OmpA) of Escherichia coli is a β‐barrel that unfolds in 8 M urea to random coil. OmpA refolds upon dilution the presence certain detergents or lipids. To examine minimal requirements for secondary and tertiary structure formation proteins, folding was studied as function hydrophobic chain length, chemical polar headgroup, concentration large array amphiphiles. folded only above critical length apolar determined by circular dichroism spectroscopy SDS‐PAGE...
The mechanism of insertion and folding an integral membrane protein has been investigated with the β-barrel forming outer A (OmpA) Escherichia coli. This work describes a new approach to this problem by combining structural information obtained from tryptophan fluorescence quenching at different depths in lipid bilayer kinetics refolding process. Experiments carried out over temperature range between 2 40 °C allowed us detect, trap, characterize previously unidentified intermediates on...
Among the major obstacles to pharmacological and structural studies of integral membrane proteins (MPs) are their natural scarcity difficulty in overproducing them native form. MPs can be overexpressed non-native state as inclusion bodies, but inducing achieve functional three-dimensional structure has proven a challenge. We describe here use an amphipathic polymer, amphipol A8-35, novel environment that allows both β-barrel α-helical fold state, absence detergents or lipids. Amphipols,...
Folding of β-barrel membrane proteins, either from a urea-unfolded form or chaperone-bound aqueous forms, has been characterized for pure lipid bilayers. The impact preinserted integral proteins biomembranes not examined in biophysical comparisons, but this knowledge is important the characterization protein assembly machinery membranes to distinguish specific effects unspecific effects. Here, folding was studied protein, outer A (OmpA) Escherichia coli, absence and presence two other BamA...
The basic biochemical and biophysical principles by which chaperone-bound membrane proteins are targeted to the outer of Gram-negative bacteria for insertion folding unknown. Here we compare spontaneous protein A (OmpA) Escherichia coli from its urea-unfolded form complex with periplasmic chaperone Skp into lipid bilayers. facilitated OmpA negatively charged membranes containing dioleoylphosphatidylglycerol (DOPG). In contrast, strongly inhibited when bilayers were composed...
An antiserum to alpha-melanocyte-stimulating hormone (alpha-MSH) was found contain antibodies at least two types of determinants on the alpha-MSH peptide: one is present only free peptide, other shared with neurofilaments. Immunoblots from mouse brain showed neurofilament crossreactivity be located proteins in Mr 140,000 range. The neurofilament-crossreactive portion could selectively absorbed out a cytoskeletal preparation, which abolished all affinity retina but did not affect labeling...