+ Site Statistics
References:
54,258,434
Abstracts:
29,560,870
PMIDs:
28,072,757
+ Search Articles
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ PDF Full Text
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Translate
+ Recently Requested

Computation of the parameters of chemical compounds binding with serum albumin based on the degree of completion of conformational changes in the protein molecule



Computation of the parameters of chemical compounds binding with serum albumin based on the degree of completion of conformational changes in the protein molecule



Farmakologiya i Toksikologiya 45(2): 122-126



A new linear expression of low mass action for computation of binding parameters which is based on the data of completeness of conformational changes in the protein molecule is proposed. These data may also be obtained by spectrofluorometry or other methods. This mode of computation allows one to show the presence of specific receptors on the protein molecule, determining adaptive structural changes in protein preceding ligand fixation.

(PDF emailed within 1 workday: $29.90)

Accession: 005024621

Download citation: RISBibTeXText


Related references

Computation of the parameters of complex formation of chemical compounds with serum albumin according to the degree of completeness of conformational transitions ion the protein molecule. Farmakologiia i Toksikologiia 45(2): 122-126, 1982

The binding of 3,6-disubstituted bile salts to human serum albumin induces conformational change on the molecule of this protein. Biochimica et Biophysica Acta 1429(2): 299-306, Jan 11, 1999

Raman studies of bovine serum albumin ionic detergent complexes and conformational change of albumin molecule induced by detergent binding. Biochimica et Biophysica Acta 703(1): 11-16, 1982

Raman studies of bovine serum albumin-ionic detergent complexes and conformational change of albumin molecule induced by detergent binding. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology 703(1): 11-16, 1982

A fluorescence-based high throughput assay for the determination of small molecule-human serum albumin protein binding. Analytical and Bioanalytical Chemistry 406(7): 1867-1875, 2014

Role of binding capacity versus binding strength in the separation of chiral compounds on protein-based high-performance liquid chromatography columns. Interactions of D- and L-tryptophan with human serum albumin. Journal of Chromatography A 725(2): 273-285, 1996

Increased degradation of albumin in cancer is not due to conformational or chemical modifications in the albumin molecule. Journal of Surgical Research 49(1): 23-29, 1990

Protein stability, conformational change and binding mechanism of human serum albumin upon binding of embelin and its role in disease control. Journal of Photochemistry and Photobiology. B, Biology 160: 248-259, 2017

Interaction of fisetin with human serum albumin by fluorescence, circular dichroism spectroscopy and DFT calculations: binding parameters and conformational changes. Journal of Luminescence 131(8): 1629-1635, 2011

Anion binding centres of human serum albumin during the n f conformational transition in isolated albumin and blood serum. Biophysics (English Translation of Biofizika) 36(3): 502-505, 1991

Probing conformational changes of human serum albumin due to unsaturated fatty acid binding by chemical cross-linking and mass spectrometry. Biochemical Journal 387(Pt 3): 695-702, 2004

Flavor protein interactions. Binding of carbonyls to bovine serum albumin: thermodynamic and conformational effects. Journal of Agricultural and Food Chemistry 28(3): 567-571, 1980

Specific interaction of chalcone-protein: cardamonin binding site II on the human serum albumin molecule. Biopolymers 79(1): 48-57, 2005

Protein binding of small molecules. V. Binding of bromphenol blue by chemical modifications of human serum albumin. Biochimica et Biophysica Acta 371(2): 451-461, 1974

The interaction of human serum albumin with selected lanthanide and actinide ions: Binding affinities, protein unfolding and conformational changes. Biochimie 123: 117-129, 2016