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In general, if the atoms that make up the ring contain heteroatoms, such rings become heterocycles, and organic compounds containing heterocycles are called heterocyclic compounds. An article called Evaluation of chemical cross-linkers for in-depth structural analysis of G protein-coupled receptors through cross-linking mass spectrometry, published in 2020-03-15, which mentions a compound: 70539-42-3, Name is Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, Molecular C18H20N2O12, Related Products of 70539-42-3.

Chem. crosslinking would conceivably cause structural disruption of a protein, but few cross-linkers have been fully evaluated in this aspect. Furthermore, integral membrane proteins may differ from soluble proteins in the selection of suitable cross-linkers, which has never been investigated. In this study, we systematically evaluated the impact of five conventional cross-linkers targeting Lys, Asp and Glu, and two Arg-reactive cross-linkers on the structural and functional integrity of two G protein-coupled receptors (GPCRs). Perturbation of the receptor structure and ligand-binding activity was observed, depending on the receptor and crosslinking conditions. In particular, our study demonstrated that the concentrations of PDH and KArGO need to be fine-tuned in order to minimize the structural and functional disturbance of specific GPCRs. A set of amenable cross-linkers was selected to acquire the most comprehensive cross-link maps for two GPCRs. Our in-depth crosslinking mass spectrometry (CXMS) anal. has revealed dynamic features of structural regions in GPCRs that are not observable in the crystal structures. Thus, CXMS anal. of GPCRs using the expanded toolkit would facilitate structural modeling of uncharacterized receptors and gain new insights into receptor-ligand interactions.

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COA of Formula: C18H20N2O12. Aromatic compounds can be divided into two categories: single heterocycles and fused heterocycles. Compound: Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, is researched, Molecular C18H20N2O12, CAS is 70539-42-3, about Covalent affinity labeling, detergent solubilization, and fluid-phase characterization of the rabbit neutrophil formyl peptide chemotaxis receptor. Author is Marasco, Wayne A.; Becker, Kathleen M.; Feltner, Douglas E.; Brown, C. Susan; Ward, Peter A.; Nairn, Roderick.

The formyl peptide chemotaxis receptor of rabbit neutrophils and purified rabbit neutrophil plasma membranes was identified by several affinity labeling techniques: (1) covalent affinity crosslinking of N-formyl-Nle-Leu-Phe-Nle-125I-Tyr-Lys (125I-hexapeptide) to the membrane-bound receptor with either di-Me suberimidate or ethylene glycol bis(succinimidyl succinate) and (2) photoactivation of N-formyl-Nle-Leu-Phe-Nle-125I-Tyr-Lys-Nε-6-[(4-azido-2-nitrophenyl)amino]hexanoate (125I-PAL). These techniques specifically identify the receptor as a polypeptide that migrates as a broad band on SDS-polyacrylamide electrophoresis, with a mol. weight (Mr) 50,000-65,000. The receptor was solubilized in active form from rabbit neutrophil membranes by using the detergents 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS) and digitonin, and from whole cells with CHAPS. Chemotaxis receptor activity was measured by the ability of the solubilized membrane material to bind 125I-hexapeptide or N-formyl-Met-Leu-[3H]Phe with gel filtration or rapid filtration through poly(ethylenimine) (PEI)-treated filters as assay systems. 125I-PAL was specifically crosslinked to the same mol. weight material in the CHAPS and digitonin solubilized extract, but no specific labeling of the receptor was seen when membranes were extracted with Nonidet P-40 and Triton X-100. Therefore, although a large number of detergents are able to solubilize the receptor, apparently some detergents release the receptor in an inactive form. The ligand binding characteristics of formyl-Met-Leu-[3H]Phe to the CHAPS-solubilized receptor shared properties with the membrane-bound formyl peptide receptor, both of which showed curvilinear, concave-upward Scatchard plots. Computer curve fitting with the program NONLIN and statistical analyses of the binding data indicated that for both the membrane-bound and solubilized receptors a 2-saturable sites model fitted the data significantly better than did a 1-saturable site model. The characteristics of the 2-saturable sites model for the soluble receptor were: a high-affinity site with a KD value of 1.25 nM and a low-affinity site with a KD value of 19.77 nM. A total of 35% of the 2 sites detected was of the higher affinity. A Hill coefficient of 0.61 was observed

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The preparation of ester heterocycles mostly uses heteroatoms as nucleophilic sites, which are achieved by intramolecular substitution or addition reactions. Compound: Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate( cas:70539-42-3 ) is researched.HPLC of Formula: 70539-42-3.Ma, Xiuguang; Yuan, Dong; Diepold, Katharina; Scarborough, Tom; Ma, Jun published the article 《The Drosophila morphogenetic protein Bicoid binds DNA cooperatively》 about this compound( cas:70539-42-3 ) in Development (Cambridge, United Kingdom). Keywords: Bicoid protein cooperative DNA binding. Let’s learn more about this compound (cas:70539-42-3).

The Drosophila morphogenetic protein Bicoid, encoded by the maternal gene bicoid, is required for the development of the anterior structures in the embryo. Bicoid, a transcriptional activator containing a homeodomain, is distributed in an anterior-to-posterior gradient in the embryo. In response to this gradient, the zygotic gene hunchback is expressed uniformly in the anterior half of the embryo in a nearly all-or-none manner. In this report we demonstrate that a recombinant Bicoid protein binds cooperatively to its sites within a hunchback enhancer element. A less than 4-fold increase in Bicoid concentration is sufficient to achieve an unbound/bound transition in DNA binding. Using various biochem. and genetic methods we further demonstrate that Bicoid mols. can interact with each other. Our results are consistent with previous studies performed in the embryo, and they suggest that one mechanism to achieve a sharp on/off switch of gene expression in response to a morphogenetic gradient is cooperative DNA binding facilitated by protein-protein interaction.

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In organic chemistry, atoms other than carbon and hydrogen are generally referred to as heteroatoms. The most common heteroatoms are nitrogen, oxygen and sulfur. Now I present to you an article called Crosslinking of the ryanodine receptor/Ca2+ release channel from skeletal muscle, published in 1995-07-26, which mentions a compound: 70539-42-3, mainly applied to ryanodine receptor crosslinking muscle, Recommanded Product: 70539-42-3.

The relationship between the tetrameric organization of the ryanodine receptor (RyR) and its activity in binding of ryanodine was approached through crosslinking studies using several bifunctional reagents, differing in their linear dimensions and flexibility, as well as in the reactivity of the active groups. Crosslinking with: 1,5-difluoro-2,4-dinitrobenzene (DFDNB); di(fluoro-3-nitrophenyl)sulfone (DFNPS), 1-ethyl-3-(3-(dimethylamino)propyl)carbodiimide (EDC); di-Me suberimidate (DMS); ethylene glycol bis(succinimidyl succinate) (EGS); and glutaraldehyde resulted in the disappearance of the, 470 kDa, RyR monomer protein band with concomitant appearance of addnl. bands of mol. masses higher than the monomer. At the relatively low concentrations of the reagents and the conditions used, RyR is the only cross-linked protein of SR membranes. The ‘new’ protein bands cross-react with antibodies against the RyR and correspond to dimers and tetramers of the RyR subunits while trimers were not detectable. DFDNB and DFNPS produced also a 560 kDa protein band which probably represents an intramol. cross-linked monomer. The SDS-electrophoretic patterns of the cross-linked purified RyR resemble those of the membrane-bound receptor. Ryanodine binding to the high-affinity site was inhibited by modification of SR membranes with DFDNB and DFNPS, but not with DMS, EDC, EGS and glutaraldehyde, although RyR was completely cross-linked. The inhibition by DFDNB and DFNPS is due to modification of a specific lysyl residue which is also involved in the control of Ca2+ release. On the other hand, cross linking of the RyR with glutaraldehyde or EGS resulted in inhibition of ryanodine binding to the low-affinity, but not to the high-affinity binding sites. Thus, the crosslinking of two or more sites in each monomer (which lead to fixation of dimers or tetramers) did not prevent the conformational changes involved in the binding and occlusion of ryanodine at the high-affinity site, but inhibited its binding to the low-affinity sites.

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The three-dimensional configuration of the ester heterocycle is basically the same as that of the carbocycle. Compound: Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate(SMILESS: O=C(ON1C(CCC1=O)=O)CCC(OCCOC(CCC(ON2C(CCC2=O)=O)=O)=O)=O,cas:70539-42-3) is researched.Recommanded Product: 70539-42-3. The article 《Tissue distribution of indium-111-labeled human monoclonal antibody (16.88) in nude mice bearing tumor xenografts: effect of diester linkage》 in relation to this compound, is published in Antibody, Immunoconjugates, and Radiopharmaceuticals. Let’s take a look at the latest research on this compound (cas:70539-42-3).

A human IgM anticolorectal monoclonal antibody 16.88 was coupled to DTPA using a diester linkage in an attempt to reduce retention of radioactivity in normal organs of animals receiving the 111In-labeled conjugate. For comparison, a 16.88-DTPA conjugate with a peptide linkage was also prepared The diester and peptide conjugates contained 3.4 and 4.3 mols. of DTPA per 16.88, resp., and their immunoreactivity was >90% as assessed by a direct-cell binding assay. Biodistribution studies in nude mice bearing THO human colon tumor xenografts indicated that diester linked conjugate was retained to a lesser extent in tumor and normal organs such as liver and kidney as compared to the peptide conjugate. The clearance of the diester conjugate from blood, however, was much faster than that of the peptide conjugate. This resulted in 2-fold higher tumor-to-serum ratio for the diester conjugate than for the peptide conjugate.

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SDS of cas: 70539-42-3. The mechanism of aromatic electrophilic substitution of aromatic heterocycles is consistent with that of benzene. Compound: Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, is researched, Molecular C18H20N2O12, CAS is 70539-42-3, about Isotopically coded cleavable cross-linker for studying protein-protein interaction and protein complexes. Author is Petrotchenko, Evgeniy V.; Olkhovik, Vyacheslav K.; Borchers, Christoph H..

An emerging approach for studying protein-protein interaction in complexes is the combination of chem. crosslinking and mass spectrometric anal. of the cross-linked peptides (cross-links) obtained after proteolysis of the complex. This approach, however, has several challenges and limitations, including the difficulty of detecting the cross-links, the potential interference from noninformative “”cross-linked peptides”” (dead end and intrapeptide cross-links), and unambiguous identification of the cross-links by mass spectrometry. Thus, the authors have synthesized an isotopically coded ethylene glycol bis(succinimidylsuccinate) derivate (D12-EGS), which contains 12 deuterium atoms for easy detection of cross-links when applied in a 1:1 mixture with its H12 counterpart and is also cleavable for releasing the cross-linked peptides allowing unambiguous identification by MS sequencing. Moreover, hydrolytic cleavage permits rapid distinguishing between different types of cross-links. Cleavage of a dead end cross-link produces a doublet with peaks 4.03 Da apart, with the lower peak appearing at a mol. mass 162 Da lower than the mass of the H12 form of the original cross-linked peptide. Cleavage of an intrapeptide cross-link leads to a doublet 8.05 Da apart and 62 Da lower than the mol. mass of the H12 form of the original cross-linked peptide. Cleavage of an interpeptide cross-link forms a pair of 4.03-Da doublets, with the lower mass member of each pair each shifted up from its unmodified mol. weight by 82 Da because of the attached portion of the cross-linker. All of this information has been incorporated into a software algorithm allowing automatic screening and detection of cross-links and cross-link types in matrix-assisted laser desorption/ionization mass spectra. In summary, the ease of detection of these species through the use of an isotopically coded cleavable cross-linker and the authors’ software algorithm, followed by mass spectrometric sequencing of the cross-linked peptides after cleavage, has been shown to be a powerful tool for studies of multi-component protein complexes.

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HPLC of Formula: 70539-42-3. The fused heterocycle is formed by combining a benzene ring with a single heterocycle, or two or more single heterocycles. Compound: Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, is researched, Molecular C18H20N2O12, CAS is 70539-42-3, about Chemical modification and immobilisation of laccase from Trametes hirsuta and from Myceliophthora thermophila. Author is Forde, Jessica; Tully, Elizabeth; Vakurov, Alex; Gibson, Tim D.; Millner, Paul; O’Fagain, Ciaran.

Laccase from two different source organisms, Myceliophthora thermophila and Trametes hirsuta, were subjected to chem. modification in solution by (1) two bifunctional reagents, ethylene-glycol-N-hydroxy succinimide (EGNHS) and glutaraldehyde and (2) by the monofunctional citraconic anhydride. The untreated and chem. modified forms of both enzymes were then immobilized onto three different types of mesoporous silicate (MPS) particle (MCM, CNS and SBA-15). Thermal stabilities of native, modified-soluble and immobilized laccases were then evaluated. Although the two laccases have similar lysine contents, those of M. thermophila are clearly more amenable to chem. modification. Treatment of the M. thermophila enzyme with EGNHS led to a 8.7-fold increase in thermal stability over the free soluble enzyme while glutaraldehyde gave a 5.7-fold increase. Increased activity of M. thermophila laccase occurred only with citraconic anhydride modification (a 3-fold increase), while the glutaraldehyde modification marginally increased the activity of the T. hirsuta enzyme (by 1.2-fold). Upon immobilization onto MPS, the greatest increase in stability was for the glutaraldehyde-treated M. thermophila preparation on SBA-15 (24-fold over the soluble enzyme). Chem. modification of laccase from T. hirsuta with both glutaraldehyde and EGNHS gave only a 2-fold increase in stability, increasing >4-fold upon immobilization onto SBA-15 and MCM-41/98.

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Computed Properties of C18H20N2O12. So far, in addition to halogen atoms, other non-metallic atoms can become part of the aromatic heterocycle, and the target ring system is still aromatic. Compound: Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, is researched, Molecular C18H20N2O12, CAS is 70539-42-3, about Reversible pH Lability of Cross-linked Vault Nanocapsules.

Vaults are ubiquitous, self-assembled protein nanocapsules with dimension in the sub-100 nm range that are conserved across diverse phyla from worms to humans. Their normal presence in humans at a copy number of over 10 000/cell makes them attractive as potential drug delivery vehicles. Toward this goal, bifunctional amine-reactive reagents are shown to be useful for the reversible crosslinking of recombinant vaults such that they may be closed and opened in a controllable manner.

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Quality Control of Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate. The fused heterocycle is formed by combining a benzene ring with a single heterocycle, or two or more single heterocycles. Compound: Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, is researched, Molecular C18H20N2O12, CAS is 70539-42-3, about Association of titin and myosin heavy chain in developing skeletal muscle. Author is Isaacs, W. B.; Kim, I. S.; Struve, A.; Fulton, A. B..

To understand mol. interactions that organize developing myofibrils, the biosynthesis and interaction of titin and myosin heavy chain in cultures of developing chicken leg myoblasts were examined Use of pulse-labeling, immunoprecipitation, and a reversible crosslinking procedure demonstrates that within minutes of synthesis, titin and myosin heavy chain can be chem. crosslinked into very large, detergent-resistant complexes retaining many features of intact myotubes. These complexes, predominantly of titin and myosin, occur very early in myofibrillogenesis as well as later. Apparently, synthesis and assembly of titin and myosin are temporally and spatially coordinated in nascent myofibrils, and titin mols. may help to organize sarcomere formation.

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Quality Control of Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate. Aromatic compounds can be divided into two categories: single heterocycles and fused heterocycles. Compound: Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, is researched, Molecular C18H20N2O12, CAS is 70539-42-3, about Conformational Adaptation of Apolipoprotein A-I to Discretely Sized Phospholipid Complexes. Author is Bhat, Shaila; Sorci-Thomas, Mary G.; Tuladhar, Rubina; Samuel, Michael P.; Thomas, Michael J..

The conformational constraints for apoA-I bound to recombinant phospholipid complexes (rHDL) were attained from a combination of chem. crosslinking and mass spectrometry. Mol. distances were then used to refine models of lipid-bound apoA-I on both 80 and 96 Å diameter rHDL particles. To obtain mol. constraints on the protein bound to phospholipid complexes, three different lysine-selective homo-bifunctional cross-linkers with increasing spacer arm lengths (i.e., 7.7, 12.0, and 16.1 Å) were reacted with purified, homogeneous recombinant 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) apoA-I rHDL complexes of each diameter Cross-linked dimeric apoA-I products were separated from monomeric apoprotein using 12% SDS-PAGE, then subjected to in-gel trypsin digest, and identified by MS/MS sequencing. These studies aid in the refinement of our previously published mol. model of two apoA-I mols. bound to ∼150 mols. of POPC and suggest that the protein hydrophobic interactions at the N- and C-terminal domains decrease as the number of phospholipid mols. or “”lipidation state”” of apoA-I increases. Thus, it appears that these incremental changes in the interaction between the N- and C-terminal ends of apoA-I stabilize its tertiary conformation in the lipid-free state as well as allowing it to unfold and sequester discrete amounts of phospholipid mols.

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