Abstract
OPINION article Front. Oncol., 11 July 2014 | https://doi.org/10.3389/fonc.2014.00183
Highlights
It is essential to bear in mind that the native conformation of human proteins is stabilized by intra-molecular disulfide (S–S) bonds between a single or multiple polypeptide chains
The formation of S–S bonds is catalyzed by protein disulfide isomerase (PDI) [1], the activation of which is associated with a number of human diseases, such as myocardial infarction, stroke, and cancer
This is due to the fact that parafibrin has different a tertiary structure than fibrin formed with thrombin
Summary
It is essential to bear in mind that the native conformation of human proteins is stabilized by intra-molecular disulfide (S–S) bonds between a single or multiple polypeptide chains. The formation of S–S bonds is catalyzed by protein disulfide isomerase (PDI) [1], the activation of which is associated with a number of human diseases, such as myocardial infarction, stroke, and cancer. Unless proper chaperone proteins are available the accidental cleavage of S–S linkages will result in the unfolding and scrambled refolding of the polypeptide chains producing non-native species present in many degenerative diseases [2,3,4,5].
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