A5022215749- Protein purification and stability
- Monoclonal and Polyclonal Antibodies Research
- Hemoglobin structure and function
- Viral Infectious Diseases and Gene Expression in Insects
- Enzyme Structure and Function
- Glycosylation and Glycoproteins Research
- Protein Structure and Dynamics
- Analytical Chemistry and Chromatography
- Fibroblast Growth Factor Research
- Mass Spectrometry Techniques and Applications
- Heme Oxygenase-1 and Carbon Monoxide
- Nerve injury and regeneration
- Proteoglycans and glycosaminoglycans research
- Enzyme Production and Characterization
- Immune Response and Inflammation
- Blood properties and coagulation
- Photosynthetic Processes and Mechanisms
- Spectroscopy and Quantum Chemical Studies
- Virus-based gene therapy research
- Endoplasmic Reticulum Stress and Disease
- Computational Drug Discovery Methods
- Neonatal Health and Biochemistry
- Phytase and its Applications
- Groundwater flow and contamination studies
- HER2/EGFR in Cancer Research
Alliance Protein Laboratories (United States)
2007-2025
Digital Research Alliance of Canada
2001-2023
Amgen (United States)
1993-2000
University of Connecticut
1981-1996
Princeton University
1991
Stanford University
1977-1980
United Science
1978
Supercon (United States)
1978
Exposure of antibodies to low pH is often unavoidable for purification and viral clearance. The conformation stability two humanized monoclonal (hIgG4-A -B) directed against different antigens a mouse antibody (mIgG1) in 0.1M citrate at acidic were studied using circular dichroism (CD), differential scanning calorimetry (DSC), sedimentation velocity. Near- far-UV CD spectra showed that exposure these 2.7-3.9 induced only limited conformational changes, although the changes greater lower pH....
Although there is considerable evidence that signaling by the erythropoietin (EPO) receptor initiated when it dimerized binding EPO, has been previously reported soluble extracellular domains of EPO (sEPOR) are not in presence and able to form only 1:1 complexes with EPO. We have now shown unambiguously light scattering, sedimentation equilibrium, titration calorimetry two molecules sEPOR can bind a single monomer but second approximately 1000-fold weaker than first. Because this interaction...
The conformations of the NeuAcα2(I)→3Galβ1(II)→4[Fucα1(III)→3]GlcNAc-O-CH3 tetrasaccharide (sLex), in aqueous solution and bound to E-, P-, L-selectin have been determined using high resolution NMR spectroscopy. In free ligand, conformation glycosidic linkage I is disordered with {ΦI, ΨI} sampling values close {−60°, 0°}, {−100°, −50°}, {180°, 0°}. trisaccharide portion rigid characterized by {ΦII, ΨII; ΦIII, ΨIII} = {46°, 18°; 48°, 24°}. measured dissociation rates equilibrium binding...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMechanism of photoinhibition photosynthetic water oxidation by chloride depletion and fluoride substitution: a protein residueM. Baumgarten, J. S. Philo, G. C. DismukesCite this: Biochemistry 1990, 29, 48, 10814–10822Publication Date (Print):December 4, 1990Publication History Published online1 May 2002Published inissue 4 December 1990https://pubs.acs.org/doi/10.1021/bi00500a014https://doi.org/10.1021/bi00500a014research-articleACS...
A magnetic susceptometer of very high sensitivity and precision has been developed using superconducting technology. Measurements show this instrument a volume susceptibility (in SI units) Δκ=±9×10−12, 0.0001% the diamagnetism typical substance such as water. The capability measuring changes during fast reactions in solution also demonstrated. System design measurement techniques are described. magnitudes frequency spectra noise sources type analyzed compared with measured performance.
We have measured the magnetic susceptibility of liquid water over 20 to 60 °C range. By using a new instrument based on superconducting technology, we obtain precision nearly two orders magnitude higher than previous studies. Notably absent from these data is any evidence for thermal anomalies reported in several earlier The vary smoothly with temperature within ±0.0001% diamagnetism, and show no abrupt changes slope. These will be useful studies molecules aqueous solution, calibration...
The interaction of neu differentiation factor (NDF) with the extracellular domains Her2 (sHer2) and Her3 (sHer3) have been studied using native gels, light scattering, sedimentation equilibrium. full-length NDFβ2 was shown to bind sHer3 a dissociation constant 26 ± 9 nM, while it showed 1000-fold weaker binding sHer2. Taken together, these results demonstrate that NDF is high affinity ligand for Her3, but not Her2. No increase in observed upon addition sHer2 NDFβ2-sHer3 mixture. Binding did...
Stem cell factor (SCF) is a cytokine that active toward hematopoietic progenitor cells and other types, including germ cells, melanocytes, mast which express its receptor, the tyrosine kinase, Kit. SCF exists as noncovalently associated dimer at concentrations where it has been possible to study quaternary structure; stimulates dimerization autophosphorylation of Kit surface. We have used recombinant versions human extracellular domain (sKit) SCF-Kit interactions. By size exclusion...
Interactions of three neurotrophin dimers, brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and a NT-3.BDNF heterodimer with extracellular, soluble TrkB TrkC receptors were studied using native gels, light scattering, sedimentation equilibrium. These neurotrophins showed binding two per dimer, tendency to dissociate into one dimer for NT-3 the heterodimer, as determined by For TrkC, gels suggested NT-3, BDNF but not nerve growth factor. Sedimentation equilibrium revealed that...