A5004504784- Protein Interaction Studies and Fluorescence Analysis
- Analytical Chemistry and Chromatography
- Various Chemistry Research Topics
- Molecular spectroscopy and chirality
- Surfactants and Colloidal Systems
- Protein purification and stability
- Field-Flow Fractionation Techniques
- Enzyme Structure and Function
- CRISPR and Genetic Engineering
- Protein Structure and Dynamics
- Hemoglobin structure and function
- Spectroscopy and Quantum Chemical Studies
- Proteins in Food Systems
- Mass Spectrometry Techniques and Applications
- Polymer Nanocomposites and Properties
- Spectroscopy and Chemometric Analyses
- Computational Drug Discovery Methods
- Hemoglobinopathies and Related Disorders
- NMR spectroscopy and applications
- Data Visualization and Analytics
- Spectroscopy Techniques in Biomedical and Chemical Research
- Rheology and Fluid Dynamics Studies
- Advanced Physical and Chemical Molecular Interactions
- Chromosomal and Genetic Variations
- Parvovirus B19 Infection Studies
ShanghaiTech University
2023-2024
Wuhan University of Science and Technology
2024
St. John's University
1981-2009
Preface to the Second Edition. First 1. Introduction. 2. Syntheses of Macromolecular Compounds. 3. Distribution Molecular Weight. 4. Thermodynamics. 5. Chain Configuration. 6. Liquid Crystals. 7. Rubber Elasticity. 8. Viscosity and Viscoelasticity. 9. Osmotic Pressure. 10. Diffusion. 11. Sedimentation. 12. Optical Rotatory Dispersion Circular Dichroism. 13. High-Performance Chromatography Electrophoresis. 14. Light Scattering. 15. Fourier Series. 16. Small-Angle X-Ray Scattering, Neutron...
We have studied the reaction K+NaCl→KCl+Na using classical trajectory techniques on an analytic potential energy surface fit to ground-state semiempirical pseudopotential of Roach and Child. A total 8000 trajectories were calculated in order study product angular distributions, partitioning complex lifetimes as a function collision energy. The ``snarled'' trajectories, shapes center-of-mass disposal all provide evidence that proceeds via formation subsequent decomposition long-lived...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTBovine Serum Albumin in Water-Dioxane MixturesK. E. Van Holde and S. F. SunCite this: J. Am. Chem. Soc. 1962, 84, 1, 66–72Publication Date (Print):January 1962Publication History Published online1 May 2002Published inissue 1 January 1962https://pubs.acs.org/doi/10.1021/ja00860a017https://doi.org/10.1021/ja00860a017research-articleACS PublicationsRequest reuse permissionsArticle Views115Altmetric-Citations16LEARN ABOUT THESE METRICSArticle Views are...
Intrinsic viscosity measurements were carried out with a polystyrene (M̄w3.2×106, M̄w/M̄n=1.03) in cyclohexane at temperatures near and including θ down to the point before precipitation occurs. The transition of coil conformation from state collapse seems be relatively smooth. onset is estimated 32.9 °C.
Measurements of light scattering at 546 nm were carried out on bovine serum albumin in LiCl solutions neutral pH (ca. 5.2) and room temperature. The concentration varied from 0.1 to 7.0 M. There was a relatively small increase the molecular weight protein when aqueous range between M 3.0 A major occurred exceeded Preferential binding same direction: negative below positive above reaction pattern suggested that aggregation is preceded by reversible conformational change monomer combination...
The circular dichroism of bovine serum albumin in divalent salt solutions was investigated. salts selected were magnesium chloride and calcium chloride. Their effects on the secondary tertiary structures protein compared with that lithium It is well known elements Ca, Mg, Li have many properties common. results show similarity their ions capacity deforming protein, spite characteristic pharmacological functions.
The physical state of bovine serum albumin in LiCl solutions at the pH near isoelectric point and room temperature has been studied with intrinsic viscosity, optical rotatory dispersion, circular dichroism ultraviolet absorption difference spectra. results indicate that effects Li+ take place two processes. 1. At concentration below 4.0 M, only general electrostatic effect occurs. There is no conformational change protein. 2. above a specific occurs which both secondary tertiary structures...
GRP94, an ER paralog of the heat-shock protein 90 family, binds and hydrolyses ATP to chaperone folding maturation its selected clients. Compared with other hsp90 proteins, in-solution conformational dynamics GRP94 along hydrolysis cycle are less understood, hindering our understanding chaperoning mechanism. Leveraging small-angle X-ray scattering, negative-staining EM, hydrogen–deuterium exchange coupled mass-spec, here we show that in apo form, ∼60% mouse (mGRP94) populates “extended”...
Difference spectra of tyrosyl residues in bovine serum albumin produced by three organic solvents (ethanol, n-propanol, and dioxane) have been studied at different pH values (pH 2.2, 5.4–5.8, 11.6). The measurements were taken 25 °C ionic strength 0.03 a concentration solvent from 5% to 25% volume. are compared those model chromophore, N-acetyl-L-tyrosine ethyl ester. Both n-propanol dioxane cause change the conformation protein, while ethanol does not. Near isoelectric point difference (at...
The effects of Li+ and H 3 O+ on the conformation bovine serum albumin in aqueous solutions at room temperature are compared. At low pH (high concentration O+) change protein is demonstrated by an increase effective volume, a decrease helical content blue shift tyrosyl residue. A similar observed for highly concentrated LiCl solution (6.0–7.0 M) neutral pH. However, 12,000 times more powerful than destabilizing molecule. This consistent with their thermodynamic kinetic properties, since...