Patrick Cramer Anton Meinhart, Tobias Silberzahn and
... Applied Science) incubation on ice for 20 min. The slurry was cleared by centrifugation, and the supernatant was loaded onto a nickel-nitrilotriacetic acid-agarose column (Qiagen). The column was washed with 20 column volumes (CV) of buffer A followed by 5 CV of buffer B (buffer A but with 300 mM Na ...
... Applied Science) incubation on ice for 20 min. The slurry was cleared by centrifugation, and the supernatant was loaded onto a nickel-nitrilotriacetic acid-agarose column (Qiagen). The column was washed with 20 column volumes (CV) of buffer A followed by 5 CV of buffer B (buffer A but with 300 mM Na ...
ATP-binding site as a further application of neural network
... interact with ATP. It may be noted that DNA-binding proteins, well known to interact through their Arg and Lys residues do not show a high propensity for His, which is observed in ATP-binding sites. This anomaly i. e. a similarity with Arg and Lys and difference from His residues may be either due t ...
... interact with ATP. It may be noted that DNA-binding proteins, well known to interact through their Arg and Lys residues do not show a high propensity for His, which is observed in ATP-binding sites. This anomaly i. e. a similarity with Arg and Lys and difference from His residues may be either due t ...
Full Text - J
... sample concentration. Determining the optimal conditions for the purification and storage of the toxins was the key step in characterizing them. It was found that ion-exchange chromatography, but not an ultrafiltration system, was suitable for concentrating toxins. We also found that the purified sa ...
... sample concentration. Determining the optimal conditions for the purification and storage of the toxins was the key step in characterizing them. It was found that ion-exchange chromatography, but not an ultrafiltration system, was suitable for concentrating toxins. We also found that the purified sa ...
Contribution of defined amino acid residues to the immunogenicity
... STh have been mapped to a highly conserved domain including six cysteine residues forming three intramolecular disul¢de bonds that are absolutely necessary for toxicity of the molecule [5]. Because STa is non-immunogenic in its native form, several di¡erent approaches have been explored to obtain no ...
... STh have been mapped to a highly conserved domain including six cysteine residues forming three intramolecular disul¢de bonds that are absolutely necessary for toxicity of the molecule [5]. Because STa is non-immunogenic in its native form, several di¡erent approaches have been explored to obtain no ...
Cell and Molecular Biology
... rich with hydrophobic amino acids is often located at the N-terminus. •Since the ribosome masks about 30 amino acids, the signal sequence isn’t fully exposed until the nascent polypeptide is about 50 amino acids long. •SRP-ribosome attaches to SRP receptor and then docks on a protein translocator. • ...
... rich with hydrophobic amino acids is often located at the N-terminus. •Since the ribosome masks about 30 amino acids, the signal sequence isn’t fully exposed until the nascent polypeptide is about 50 amino acids long. •SRP-ribosome attaches to SRP receptor and then docks on a protein translocator. • ...
Molecule of the Month: AgrA DNA Binding Domain AgrA is the
... Because of its role within the Agr system, AgrA seems to be the most appealing drug target. As with all two component signaling systems in bacteria, the Agr system contains both a histidine kinase (AgrC) and a response regulator (AgrA) (Figure 1). The other components of the system (AgrB and AgrD) f ...
... Because of its role within the Agr system, AgrA seems to be the most appealing drug target. As with all two component signaling systems in bacteria, the Agr system contains both a histidine kinase (AgrC) and a response regulator (AgrA) (Figure 1). The other components of the system (AgrB and AgrD) f ...
Structure and function of the chloroplast signal recognition particle
... formation with cpSRP. By analogy, with the co-translational targeting system where binding of cytosolic SRP54 to a substrate protein is mediated via its hydrophobic signal sequence, it was shown that a hydrophobic domain within LHCP is required for the post-translational binding to cpSRP (DeLille et ...
... formation with cpSRP. By analogy, with the co-translational targeting system where binding of cytosolic SRP54 to a substrate protein is mediated via its hydrophobic signal sequence, it was shown that a hydrophobic domain within LHCP is required for the post-translational binding to cpSRP (DeLille et ...
Bacteria Binding by DMBT1/SAG/gp-340 Is Confined to
... (8), the SRCR domain of MSR1 does not seem to be involved in bacteria binding (9, 10). Bacteria binding by MARCO involves an RXR motif within the SRCR domain, indicating that ionic interactions play a crucial role in the interaction with its negatively charged ligands (6). Group B SRCR proteins are ...
... (8), the SRCR domain of MSR1 does not seem to be involved in bacteria binding (9, 10). Bacteria binding by MARCO involves an RXR motif within the SRCR domain, indicating that ionic interactions play a crucial role in the interaction with its negatively charged ligands (6). Group B SRCR proteins are ...
IOSR Journal of Pharmacy and Biological Sciences (IOSR-JPBS)
... not have any clear ATP- or GTP-specific binding motif. Although the active site residues are mostly conserved in all PEPCK, not much significant sequence homology persists between ATP and GTP dependent PEPCK enzymes. There is only one planctomycetes PEPCK enzyme (from Cadidatus Kuenenia stuttgartien ...
... not have any clear ATP- or GTP-specific binding motif. Although the active site residues are mostly conserved in all PEPCK, not much significant sequence homology persists between ATP and GTP dependent PEPCK enzymes. There is only one planctomycetes PEPCK enzyme (from Cadidatus Kuenenia stuttgartien ...
Trends in Plant Science
... within a protein domain family could be low and might only be conserved in some crucial functional residues (such as active sites and ligand-binding sites) (Fig. 1b). This explains why the presence of a particular domain in a protein could be overlooked during searches, as a result of ‘masking’ by t ...
... within a protein domain family could be low and might only be conserved in some crucial functional residues (such as active sites and ligand-binding sites) (Fig. 1b). This explains why the presence of a particular domain in a protein could be overlooked during searches, as a result of ‘masking’ by t ...
5-Cell and Molecular Biology (Golgi etc)
... These oligosaccharide processing pathways occur in a correspondingly organized sequence in the Golgi stack, with each cisterna containing its own set of processing enzymes Proteins are modified in successive stages as they move from cisterna to cisterna across the stack So that the stack forms ...
... These oligosaccharide processing pathways occur in a correspondingly organized sequence in the Golgi stack, with each cisterna containing its own set of processing enzymes Proteins are modified in successive stages as they move from cisterna to cisterna across the stack So that the stack forms ...
University of Groningen Sugar transport in
... for trehalose/maltose of Thermococcus litoralis and Pyrococcus furiosus, maltodextrin of P. furiosus [14,17], and trehalose of S. solfataricus [9]. CUT2 subfamily members present in the archaeal genomes have not been characterized. The transport systems for arabinose and glucose of S. solfataricus [ ...
... for trehalose/maltose of Thermococcus litoralis and Pyrococcus furiosus, maltodextrin of P. furiosus [14,17], and trehalose of S. solfataricus [9]. CUT2 subfamily members present in the archaeal genomes have not been characterized. The transport systems for arabinose and glucose of S. solfataricus [ ...
Recombinant N-terminal Nucleotide
... product CFTR, to bacterial transporters (10). The ATPase activity and related drug transport of P-glycoprotein require both functional nucleotide-binding sites (11, 12) and are sensitive to the cysteine-specific modifier N-ethylmaleimide (NEM) (13– 17). The lack of structural data about P-glycoprote ...
... product CFTR, to bacterial transporters (10). The ATPase activity and related drug transport of P-glycoprotein require both functional nucleotide-binding sites (11, 12) and are sensitive to the cysteine-specific modifier N-ethylmaleimide (NEM) (13– 17). The lack of structural data about P-glycoprote ...
Investigation of a Zα-like Peptide Motif in Koi Herpesvirus
... of DNA. Furthermore, two changes made in the amino acid sequence of the protein caused important structural changes in the DNA. The insights into DNA-protein interaction gained in this work could aid in understanding the mechanism of KHV’s high lethality. ...
... of DNA. Furthermore, two changes made in the amino acid sequence of the protein caused important structural changes in the DNA. The insights into DNA-protein interaction gained in this work could aid in understanding the mechanism of KHV’s high lethality. ...
The potato NLR immune receptor R3a does not contain
... A recent study by Kroj et al. (New Phytologist, 2016) surveyed nucleotide binding-leucine rich repeat (NLR) proteins from plant genomes for the presence of extraneous integrated domains that may serve as decoys or sensors for pathogen effectors. They reported that a FAM75 domain of unknown function ...
... A recent study by Kroj et al. (New Phytologist, 2016) surveyed nucleotide binding-leucine rich repeat (NLR) proteins from plant genomes for the presence of extraneous integrated domains that may serve as decoys or sensors for pathogen effectors. They reported that a FAM75 domain of unknown function ...
IOSR Journal of Pharmacy and Biological Sciences (IOSR-JPBS) e-ISSN: 2278-3008, p-ISSN:2319-7676.
... The Vorapaxar binding pocket is located on the central axis of β-propeller structure and is composed of α-helical domain and long loops. These loops seem to be playing important structural role in holding and accommodating the substrate. The α-helices which are participating in the Vorapaxar binding ...
... The Vorapaxar binding pocket is located on the central axis of β-propeller structure and is composed of α-helical domain and long loops. These loops seem to be playing important structural role in holding and accommodating the substrate. The α-helices which are participating in the Vorapaxar binding ...
Protein structure is conceptually divided into four levels of organization
... barrel is lined by small hydrophilic side chains (serine and threonine) from the b strands, which creates a hole in the middle where one of the substrate molecules, coenzyme A (green), binds along the axis of the barrel from one end to the other. (Adapted from a computer-generated diagram provided b ...
... barrel is lined by small hydrophilic side chains (serine and threonine) from the b strands, which creates a hole in the middle where one of the substrate molecules, coenzyme A (green), binds along the axis of the barrel from one end to the other. (Adapted from a computer-generated diagram provided b ...
Host-Parasite Relationships
... if all Fe bound to transferrin or lactoferrin, then Fe become limiting for the bacteria Bacterial siderophores – small MW proteins containing many OH groups with VERY high affinity for Fe. Can actually strip it away from Transferrin and lactoferrin – E. coli siderophore == AEROBACTIN Once inside may ...
... if all Fe bound to transferrin or lactoferrin, then Fe become limiting for the bacteria Bacterial siderophores – small MW proteins containing many OH groups with VERY high affinity for Fe. Can actually strip it away from Transferrin and lactoferrin – E. coli siderophore == AEROBACTIN Once inside may ...
Poster for RCPSC mee.. - University of Alberta
... (GlcCer) is a metabolite of ceramide produced by the glycosylation of the 1-hydroxyl group of ceramide by the enzyme Glucosylceramide Synthase (GCS) (Figure 1). Given the similarities in structure between the natural product inhibitors of PP1, the clavosines, and the sphingolipid GlcCer, we hypothes ...
... (GlcCer) is a metabolite of ceramide produced by the glycosylation of the 1-hydroxyl group of ceramide by the enzyme Glucosylceramide Synthase (GCS) (Figure 1). Given the similarities in structure between the natural product inhibitors of PP1, the clavosines, and the sphingolipid GlcCer, we hypothes ...
The Binding Site for the @r Subunits of Heterotrimeric G Proteins on
... gene family seemed to support this concept that the GTPasecontaining a subunit was the active component of G proteins (1-3). In recent years, however, several @ and y isoforms have been isolated (3) which display specificity not only in their interaction with one another (4, 5) but in coupling speci ...
... gene family seemed to support this concept that the GTPasecontaining a subunit was the active component of G proteins (1-3). In recent years, however, several @ and y isoforms have been isolated (3) which display specificity not only in their interaction with one another (4, 5) but in coupling speci ...
Comparative Models of GABAA Receptor
... Fig. 1. Alignment of nACh and GABAA receptor helical domains. a, a subset of a superfamily alignment of the four segments that make up the helical (transmembrane) domain of the subunit chains is shown. The position of the missing “cytoplasmic loop” between helices 3 and 4 is indicated by a double-ga ...
... Fig. 1. Alignment of nACh and GABAA receptor helical domains. a, a subset of a superfamily alignment of the four segments that make up the helical (transmembrane) domain of the subunit chains is shown. The position of the missing “cytoplasmic loop” between helices 3 and 4 is indicated by a double-ga ...
Protein
... determine protein conformation. • This technique requires the formation of a crystal of the protein being studied. • The pattern of diffraction of an X-ray by the atoms of the crystal can be used to determine the location of the atoms and to build a computer model of its structure. Copyright © 2002 ...
... determine protein conformation. • This technique requires the formation of a crystal of the protein being studied. • The pattern of diffraction of an X-ray by the atoms of the crystal can be used to determine the location of the atoms and to build a computer model of its structure. Copyright © 2002 ...
Proteins
... determine protein conformation. • This technique requires the formation of a crystal of the protein being studied. • The pattern of diffraction of an X-ray by the atoms of the crystal can be used to determine the location of the atoms and to build a computer model of its structure. Copyright © 2002 ...
... determine protein conformation. • This technique requires the formation of a crystal of the protein being studied. • The pattern of diffraction of an X-ray by the atoms of the crystal can be used to determine the location of the atoms and to build a computer model of its structure. Copyright © 2002 ...
Analysis of the glycoside hydrolase family 8 catalytic core in
... The glycoside hydrolase family 8 (GH-8) consists of bifunctional cellulase-chitosanases many of which are produced by species of Bacillus. Chitosanolytic enzymes can be useful in producing low molecular weight chitooligosaccharides which have several applications. In addition, a bifunctional enzyme ...
... The glycoside hydrolase family 8 (GH-8) consists of bifunctional cellulase-chitosanases many of which are produced by species of Bacillus. Chitosanolytic enzymes can be useful in producing low molecular weight chitooligosaccharides which have several applications. In addition, a bifunctional enzyme ...
Citrate transporters of Bacillus subtilis Krom, Bastiaan Philip
... which couple translocation to chemical modification of the substrate. Best known are the bacterial phosphotransferase systems that use energy derived from the hydrolysis of phosphoenolpyruvate (PEP) for translocation of sugars. The sugar is phosphorylated during the transport process. Solute transpo ...
... which couple translocation to chemical modification of the substrate. Best known are the bacterial phosphotransferase systems that use energy derived from the hydrolysis of phosphoenolpyruvate (PEP) for translocation of sugars. The sugar is phosphorylated during the transport process. Solute transpo ...
Anthrax toxin
Anthrax toxin is a three-protein exotoxin secreted by virulent strains of the bacterium, Bacillus anthracis—the causative agent of anthrax. The toxin was first discovered by Harry Smith in 1954. Anthrax toxin is composed of a cell-binding protein, known as protective antigen (PA), and two enzyme components, called edema factor (EF) and lethal factor (LF). These three protein components act together to impart their physiological effects. Assembled complexes containing the toxin components are endocytosed. In the endosome, the enzymatic components of the toxin translocate into the cytoplasm of a target cell. Once in the cytosol, the enzymatic components of the toxin disrupts various immune cell functions, namely cellular signaling and cell migration. The toxin may even induce cell lysis, as is observed for macrophage cells. Anthrax toxin allows the bacteria to evade the immune system, proliferate, and ultimately kill the host animal. Research on anthrax toxin also provides insight into the generation of macromolecular assemblies, and on protein translocation, pore formation, endocytosis, and other biochemical processes.