V6-SecondaryStructur.. - Chair of Computational Biology
... helix residues that are correctly predicted, Q %prd2T percentage of all predicted TMH helix residues that are correctly predicted, Q%obs2N percentage of all observed non-TMH helix residues that are correctly predicted, Q%prd2N percentage of all predicted non-TMH helix residues that are correctly pre ...
... helix residues that are correctly predicted, Q %prd2T percentage of all predicted TMH helix residues that are correctly predicted, Q%obs2N percentage of all observed non-TMH helix residues that are correctly predicted, Q%prd2N percentage of all predicted non-TMH helix residues that are correctly pre ...
Questions for exam #1
... smaller. Mitochondria, which have evolved from independent cells, are much larger than most organelles, and are about the size of their bacterial ancestors (usually a few microns). MTs and tubulin are much smaller; teeth and tails are much longer. 5. Arp is a transporter that catalyzes transport of ...
... smaller. Mitochondria, which have evolved from independent cells, are much larger than most organelles, and are about the size of their bacterial ancestors (usually a few microns). MTs and tubulin are much smaller; teeth and tails are much longer. 5. Arp is a transporter that catalyzes transport of ...
pO 2
... – Monomer interactions, most chain interaction occurs between and chains » through mostly hydrophobic residues » and interactions are few and polar » and contact act as a switch ...
... – Monomer interactions, most chain interaction occurs between and chains » through mostly hydrophobic residues » and interactions are few and polar » and contact act as a switch ...
Structure - chula ise
... protein, where they can interact with water; the nonpolar amino acid side chains are buried on the inside to form a tightly packed hydrophobic core of atoms that are hidden from water. In this schematic drawing, the protein contains only about 30 amino acids. ...
... protein, where they can interact with water; the nonpolar amino acid side chains are buried on the inside to form a tightly packed hydrophobic core of atoms that are hidden from water. In this schematic drawing, the protein contains only about 30 amino acids. ...
Nature
... has been implicated in multiple diseases of the nervous system. Here we present the crystal structure of a bacterial homologue of these transporters from Aquifex aeolicus, in complex with its substrate, leucine, and two sodium ions. The protein core consists of the first ten of twelve transmembrane ...
... has been implicated in multiple diseases of the nervous system. Here we present the crystal structure of a bacterial homologue of these transporters from Aquifex aeolicus, in complex with its substrate, leucine, and two sodium ions. The protein core consists of the first ten of twelve transmembrane ...
SALT BRIDGE D526- FUNCTIONS AS A HINGE THAT CONTROLS
... misfolded proteins under heat shock conditions. They also participate in cellular processes such as folding of newly synthesized polypeptides, protein translocation across membranes, assembly and disassembly of protein complexes and refolding of protein aggregates (1). ...
... misfolded proteins under heat shock conditions. They also participate in cellular processes such as folding of newly synthesized polypeptides, protein translocation across membranes, assembly and disassembly of protein complexes and refolding of protein aggregates (1). ...
CHAPTER 6
... G proteins may either stimulate or inhibit an effector. • In the case of adenylyl cyclase, the stimulatory G protein is known as Gs and the inhibitory G protein is known as Gi • Gi may act either by the Gia subunit binding to AC or by the Gibg complex complexing all the Gsa and preventing it from bi ...
... G proteins may either stimulate or inhibit an effector. • In the case of adenylyl cyclase, the stimulatory G protein is known as Gs and the inhibitory G protein is known as Gi • Gi may act either by the Gia subunit binding to AC or by the Gibg complex complexing all the Gsa and preventing it from bi ...
Role of basic character of α-sarcin`s NH2-terminal β
... α-Sarcin is the most representative member of ribotoxins, a family of fungal natural killers characterized by their exquisite ribonucleolytic specificity against ribosomes and their ability to cross cellular membranes in the absence of any known protein receptor [1,2]. These toxic proteins cleave ju ...
... α-Sarcin is the most representative member of ribotoxins, a family of fungal natural killers characterized by their exquisite ribonucleolytic specificity against ribosomes and their ability to cross cellular membranes in the absence of any known protein receptor [1,2]. These toxic proteins cleave ju ...
Structural Insights into Catalysis and Inhibition of O
... the product is released via regeneration of the internal aldi- cleavage. Residual non-cleaved His-CysK1 was removed by pasmine. Formation of the external aldimine appears to be coupled sage through a nickel-nitrilotriacetic acid column. The flowto a large conformational change that leads to the clos ...
... the product is released via regeneration of the internal aldi- cleavage. Residual non-cleaved His-CysK1 was removed by pasmine. Formation of the external aldimine appears to be coupled sage through a nickel-nitrilotriacetic acid column. The flowto a large conformational change that leads to the clos ...
Ecological and molecular investigations of cyanotoxin production
... succession may be the result of numerous environmental conditions, such as changes in nutrient availability, light and temperature, favouring individual strains. However, with the recent identi¢cation of genes encoding eukaryotic type Ser/Thr protein kinases [32] and protein phosphatases (PPs) from ...
... succession may be the result of numerous environmental conditions, such as changes in nutrient availability, light and temperature, favouring individual strains. However, with the recent identi¢cation of genes encoding eukaryotic type Ser/Thr protein kinases [32] and protein phosphatases (PPs) from ...
Side-chain hydrophobicity scale derived from transmembrane
... transmembrane scaffold on which to introduce amino acid side chains of our choice at various membrane depths. We selected OmpLA because it: (a) spontaneously folds and inserts into lipid membranes from a solubilized unfolded state (14), (b) has a known three-dimensional structure (Fig. 1A) (15), and ...
... transmembrane scaffold on which to introduce amino acid side chains of our choice at various membrane depths. We selected OmpLA because it: (a) spontaneously folds and inserts into lipid membranes from a solubilized unfolded state (14), (b) has a known three-dimensional structure (Fig. 1A) (15), and ...
TIBS review article by Killian & Heijne
... and KALP peptides on lipid organization, one striking difference was observed: KALP peptides appeared to have a shorter effective length than WALP peptides; that is, a 23-amino-acid KALP peptide (KALP23) behaved exactly the same as a 21-amino-acid WALP peptide (WALP21). How can we explain this? In t ...
... and KALP peptides on lipid organization, one striking difference was observed: KALP peptides appeared to have a shorter effective length than WALP peptides; that is, a 23-amino-acid KALP peptide (KALP23) behaved exactly the same as a 21-amino-acid WALP peptide (WALP21). How can we explain this? In t ...
What are Membranes?
... by fluorescence microscopy, with a time resolution of 25 µs (equivalent to 40,000 frames/s). The track shown here represents a molecule followed for 56 ms (2,250 frames); the trace begins in the purple area and continues through blue, green, and orange. The pattern of movement indicates rapid diffus ...
... by fluorescence microscopy, with a time resolution of 25 µs (equivalent to 40,000 frames/s). The track shown here represents a molecule followed for 56 ms (2,250 frames); the trace begins in the purple area and continues through blue, green, and orange. The pattern of movement indicates rapid diffus ...
Topological studies suggest that the pathway of the protons through
... TID-reactive residues in F0• The labeling profilein Fig. 58 was obtaincd after reaction with Neurospora crassa mitochondria in the presence of an oligomycin concentration 10-fold higher than necessary for maximal inhibition. The identical group of residues was TID-reactive in the presence and in the ...
... TID-reactive residues in F0• The labeling profilein Fig. 58 was obtaincd after reaction with Neurospora crassa mitochondria in the presence of an oligomycin concentration 10-fold higher than necessary for maximal inhibition. The identical group of residues was TID-reactive in the presence and in the ...
FYVE-Dependent Endosomal Targeting of an Arrestin
... signaling and their trafficking. The arrestin superfamilly includes several arrestin domain-containing proteins and the structurally related protein Vps26. In Dictyostelium discoideum, the arrestin-domain containing proteins form a family of six members, namely AdcA to -F. In contrast to canonical a ...
... signaling and their trafficking. The arrestin superfamilly includes several arrestin domain-containing proteins and the structurally related protein Vps26. In Dictyostelium discoideum, the arrestin-domain containing proteins form a family of six members, namely AdcA to -F. In contrast to canonical a ...
Structure-Function Analysis of the UDP-N-acetyl-D
... essential to catalytic activity (7, 9, 11). Such carboxylic acid residues may be involved in different aspects of the catalytic process. First, glycosyltransferases (including ppGaNTases) that retain the anomeric configuration of the sugar-nucleotide bond are thought to work via a double displacemen ...
... essential to catalytic activity (7, 9, 11). Such carboxylic acid residues may be involved in different aspects of the catalytic process. First, glycosyltransferases (including ppGaNTases) that retain the anomeric configuration of the sugar-nucleotide bond are thought to work via a double displacemen ...
Sugar Transport in (Hyper-)Thermophilic Archaea
... either float free in the periplasm (Gramnegative) or are attached to the membrane via a fatty acid modification of the aminoterminus (Gram-positive) (Fig. 2). In bacteria it is also possible for the binding protein to have fused with the membrane domain, as for instance the glycine betaine ...
... either float free in the periplasm (Gramnegative) or are attached to the membrane via a fatty acid modification of the aminoterminus (Gram-positive) (Fig. 2). In bacteria it is also possible for the binding protein to have fused with the membrane domain, as for instance the glycine betaine ...
Supplemental Material
... Identification of SRCR and CTLD domains within the Chlamydomonas genome Version 3.0 of the Chlamydomonas genome was used for all analyses (http://genome.jgi-psf.org/Chlre3/Chlre3.home.html). Candidate protein domains were identified using a combination of BLAST analysis with SRCR and CTLD domains fr ...
... Identification of SRCR and CTLD domains within the Chlamydomonas genome Version 3.0 of the Chlamydomonas genome was used for all analyses (http://genome.jgi-psf.org/Chlre3/Chlre3.home.html). Candidate protein domains were identified using a combination of BLAST analysis with SRCR and CTLD domains fr ...
Tertiary Structure
... regions: residues 38 - 47, which form the loop after b strand 2, and residues 190 - 193, which form the loop after b strand 5. The tyrosine and adenylate moieties are bound on opposite sides of the b sheet outside the carboxy ends of b strands 2 and 5. ...
... regions: residues 38 - 47, which form the loop after b strand 2, and residues 190 - 193, which form the loop after b strand 5. The tyrosine and adenylate moieties are bound on opposite sides of the b sheet outside the carboxy ends of b strands 2 and 5. ...
Structural Insights into Maize Viviparous14, a Key
... Drought, cold, and/or high salinity induce an increase in VP14 activity. The resulting elevation of ABA levels leads to the appropriate biological responses. ...
... Drought, cold, and/or high salinity induce an increase in VP14 activity. The resulting elevation of ABA levels leads to the appropriate biological responses. ...
evaluation of cirrhosis liver disease via protein-protein
... analysis undergo EXPASy , STRING Database and DAVID Bioinformatics Resources query. Based on GO analysis, the most of the proteins are located in endoplasmic reticulum lumen, intracellular organelle lumen, membrane-enclosed lumen and extracellular region. Actin binding, metal ion binding, cation bin ...
... analysis undergo EXPASy , STRING Database and DAVID Bioinformatics Resources query. Based on GO analysis, the most of the proteins are located in endoplasmic reticulum lumen, intracellular organelle lumen, membrane-enclosed lumen and extracellular region. Actin binding, metal ion binding, cation bin ...
Exam 2
... triphosphate chain using 5’ carbons on each. c) The phosphate “to the right” of the A is on the 3’ carbon. d) The atom that is methylated on guanine then carries a positive charge. Draw the molecular structure of this “cap” (at pH 7). Do not “abbreviate” the ...
... triphosphate chain using 5’ carbons on each. c) The phosphate “to the right” of the A is on the 3’ carbon. d) The atom that is methylated on guanine then carries a positive charge. Draw the molecular structure of this “cap” (at pH 7). Do not “abbreviate” the ...
Mutation of exposed hydrophobic amino acids to arginine to
... The effect of mutations on stability was homogeneous, a mutation either destabilizes or stabilizes the protein since we never found a mutation which significantly stabilizes the protein for one agent and significantly destabilizes it for another. Most of the mutations significantly affect the stabil ...
... The effect of mutations on stability was homogeneous, a mutation either destabilizes or stabilizes the protein since we never found a mutation which significantly stabilizes the protein for one agent and significantly destabilizes it for another. Most of the mutations significantly affect the stabil ...
Comparisons between the Primary Structure of the Coat Proteins of
... of the crosslinked virions. Carbon-13 nuclear magnetic resonance studies have shown that in another tymovirus, belladonna mottle virus, glutamic and aspartic residues are in contact with the RNA (Virudachalam et al., 1983): two aspartic acid residues are conserved in all three sequences, at position ...
... of the crosslinked virions. Carbon-13 nuclear magnetic resonance studies have shown that in another tymovirus, belladonna mottle virus, glutamic and aspartic residues are in contact with the RNA (Virudachalam et al., 1983): two aspartic acid residues are conserved in all three sequences, at position ...
Membrane Proteins
... • Most of protein (N-terminal portion) on outside of cell, exposed to water; mainly hydrophilic residues, heavily glycosylated (carbohydrates in glycosidic bonds to Ser, Thr, and Asn) • Carbohydrates: ABO and MN blood group antigen-determining structures. • Extracellular part of protein also recepto ...
... • Most of protein (N-terminal portion) on outside of cell, exposed to water; mainly hydrophilic residues, heavily glycosylated (carbohydrates in glycosidic bonds to Ser, Thr, and Asn) • Carbohydrates: ABO and MN blood group antigen-determining structures. • Extracellular part of protein also recepto ...
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.