Effect of oxidative sulfitolysis of disulfide bonds of bovine serum albumin on its structural properties: A physicochemical study

1988 ◽  
Vol 7 (5) ◽  
pp. 535-548 ◽  
Author(s):  
Navin Kumar D. Kella ◽  
Yeung J. Kang ◽  
John E. Kinsella
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Structural Properties ◽  
Bovine Serum ◽  
Disulfide Bonds ◽  
Physicochemical Study

scholarly journals Physicochemical study of biomolecular interactions between lysosomotropic surfactants and bovine serum albumin

2017 ◽  
Vol 159 ◽  
pp. 750-758 ◽  
Author(s):  
Tomasz Janek ◽  
Żaneta Czyżnikowska ◽  
Jacek Łuczyński ◽  
Eduardo J. Gudiña ◽  
Lígia R. Rodrigues ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Physicochemical Study ◽  
Biomolecular Interactions

The effect of putrescine on stability and structural properties of bovine serum albumin

2020 ◽  
Vol 39 (1) ◽  
pp. 254-262
Author(s):  
Elham Ziaee ◽  
Behzad Shareghi ◽  
Sadegh Farhadian ◽  
Lida Momeni ◽  
Fatemeh Heibati-Goojani
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Structural Properties ◽  
Bovine Serum

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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