The Availability of the Disulfide Bonds of Human and Bovine Serum Albumin and of Bovine γ-Globulin to Reduction by Thioglycolic Acid

1957 ◽  
Vol 79 (15) ◽  
pp. 4096-4099 ◽  
Author(s):  
Ephraim Katchalski ◽  
George S. Benjamin ◽  
Violet Gross
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Disulfide Bonds ◽  
Thioglycolic Acid

Bis(triethylphosphine)gold(I) chloride: ionization in aqueous solution, reduction in vitro of the external and internal disulfide bonds of bovine serum albumin and antiarthritic activity

1989 ◽  
Vol 28 (7) ◽  
pp. 1321-1326 ◽  
Author(s):  
Anvarhusein A. Isab ◽  
Anne L. Hormann ◽  
David T. Hill ◽  
Don E. Griswold ◽  
Michael J. DiMartino ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Disulfide Bonds

scholarly journals An All-Atomistic Molecular Dynamics Study to Determine the Structural Importance of Disulfide Bonds in Immunoglobulin G and Bovine Serum Albumin

2018 ◽  
Vol 15 (1) ◽  
Author(s):  
Akshay Mathavan ◽  
Akash Mathavan ◽  
Michael Fortunato ◽  
Coray Colina
Keyword(s):  
Molecular Dynamics ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Immunoglobulin G ◽  
Bovine Serum ◽  
Disulfide Bonds ◽  
Structural Changes ◽  
Conformational Stability ◽  
The Stability

A fully-atomistic molecular dynamics study was performed to determine the importance of disulfide bonds on the stability of immunoglobulin G (IgG) and bovine serum albumin (BSA).The transferability of a previous prescreening methodology to assess contributions from individual disulfide bonds on conformational stability was tested on both proteins. In IgG, it was apparent that inter-chain and intra-chain disulfide bonds play different roles in maintaining structure, evidenced by clear separation of inter-chain cysteine residues upon cleavage of disulfide bonds. In BSA, a set of double disulfide bonds required both to be broken in order to observe significant structural changes, equivalently seen in a previous study of human serum albumin (HSA), a structurally similar protein. Structural analysis of IgG showed deviations in distances between domains, while analysis of BSA suggested more local structural changes. This work helps confirm the efficacy and reproducibility of the prescreening methodology on both a novel, larger protein such as IgG and a more homologous (to HSA), globular protein such as BSA. The results provide insight into the role of specific disulfide bonds in the stability of IgG and BSA. KEYWORDS: Molecular Dynamics; Atomistic Simulations; Immunoglobulin G; Bovine Serum Albumin; Disulfide Bonds

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