Multiple Disulfide-Bonded States of Native Proteins: Estimate of Number Using Probabilities of Disulfide Bond Formation

Multiple Disulfide-Bonded States of Native Proteins: Estimate of Number Using Probabilities of Disulfide Bond Formation.

Full text not available from this repository.
Item Type: Article
Status: Published
Official URL: https://doi.org/10.3390/molecules25235729
Journal or Publication Title: Molecules
Volume: 25
Number: 23
Page Range: p. 5729
Date: 2020
Divisions: ACRF Centenary Cancer Research Centre
Depositing User: General Admin
Identification Number: 10.3390/molecules25235729
ISSN: 1420-3049
Date Deposited: 05 Jan 2021 05:07
Abstract:

The polypeptide backbone of proteins is held together by two main types of covalent bonds: the peptide bonds that link the amino acid residues and the disulfide bonds that link pairs of cysteine amino acids. Disulfide bonds form as a protein folds in the cell and formation was assumed to be complete when the mature protein emerges. This is not the case for some secreted human blood proteins. The blood clotting protein, fibrinogen, and the protease inhibitor, α2-macroglobulin, exist in multiple disulfide-bonded or covalent states in the circulation. Thousands of different states are predicted assuming no dependencies on disulfide bond formation. In this study, probabilities for disulfide bond formation are employed to estimate numbers of covalent states of a model polypeptide with reference to α2-macroglobulin. When disulfide formation is interdependent in a protein, the number of covalent states is greatly reduced. Theoretical estimates of the number of states will aid the conceptual and experimental challenges of investigating multiple disulfide-bonded states of a protein.

Creators:
Creators
Email
Hogg, Philip J.
UNSPECIFIED
Last Modified: 05 Jan 2021 05:07
URI: https://eprints.centenary.org.au/id/eprint/911

Actions (login required)

View Item View Item