A bioinformatics study on characteristics, metabolic pathways, and cellular functions of the identified S-nitrosylated proteins in postmortem pork muscle

Effect of Nitric Oxide and Its Induced Protein S-Nitrosylation on the Structures and In Vitro Digestion Properties of Beef Myofibrillar Protein

“…The α-helix content significantly decreased while the β-turn content dramatically increased, demonstrating that NO and its mediated protein S-nitrosylation could induce proteins to have a transition from ordered to disordered structures. Previous studies have found that the S-nitrosocysteine residues were mainly located in the α-helix, β-sheet, and β-turn of the secondary structure . The reduced α-helix content might be a direct result of the protein S-nitrosylation.…”

“…Previous studies have found that the S-nitrosocysteine residues were mainly located in the α-helix, β-sheet, and β-turn of the secondary structure. 15 The reduced α-helix content might be a direct result of the protein S-nitrosylation. Derakhshan et al 1 found that the Cys132 site of argininosuccinate synthetase was located in the α-helix structure of the protein.…”

“…The digestibility of proteins is influenced by physicochemical changes in proteins which could affect the site of action of digestive enzymes, thus altering digestibility . Liu et al indicated that the modified cysteine sites were mainly distributed in the α-helix, β-sheet, and β-turn, which were located in the functional region of the secondary structure . MP had a different degradation pattern under S-nitrosoglutathione (GSNO) treatment, possibly because protein S-nitrosylation led to a change in protein structure that exposes more degradation sites to the enzyme calpain-1.…”

“…14 Liu et al indicated that the modified cysteine sites were mainly distributed in the α-helix, β-sheet, and β-turn, which were located in the functional region of the secondary structure. 15 MP had a different degradation pattern under S-nitrosoglutathione (GSNO) treatment, possibly because protein S-nitrosylation led to a change in protein structure that exposes more degradation sites to the enzyme calpain-1. Kumari et al 16 also showed that S-nitrosylation of the deubiquitinating enzyme (OTUB1) increased the β-sheet content from 32.6% (OTUB1, 37 °C) to 39.0% (OTUB1 1:10 GSNO) and decreased the α-helix content from 18.0% (OTUB1, 37 °C) to 11.0% (OTUB1 1:10 GSNO) in a concentration-dependent manner, disrupted its native structure, and promoted amyloid aggregation.…”

Protein S-Nitrosylation Regulates Postmortem Beef Apoptosis through the Intrinsic Mitochondrial Pathway

“…20 Besides, most of the S-nitrosylated proteins were in the range of 25−55 kDa, revealing that low-molecular proteins were more susceptible to S-nitrosylation. The result agrees with the finding of Liu et al 21 that most S-nitrosylated proteins were distributed within 100 kDa, specifically around 40−60 kDa. In addition, no significant difference in the number of Snitrosylated protein bands was noted among the three groups.…”