Oxidative Folding of Proteins
Bok Engelsk
| Medvirkende | Feige, Matthias J., (Editor.)
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| Utgitt | Royal Society of Chemistry
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| Omfang | 1 online resource (429 p.)
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| Opplysninger | The formation of disulphide bonds is probably the most influential modification of proteins. These bonds are unique among post-translational modifications of proteins as they can covalently link cysteine residues far apart in the primary sequence of a protein. This has the potential to convey stability to otherwise marginally stable structures of proteins. However, the reactivity of cysteines comes at a price: the potential to form incorrect disulphide bonds, interfere with folding, or even cause aggregation. An elaborate set of cellular machinery exists to catalyze and guide this process: facilitating bond formation, inhibiting unwanted pairings and scrutinizing the outcomes. Only in recent years has it become clear how intimately connected this cellular machinery is with protein folding helpers, organellar redox balance and cellular homeostasis as a whole.
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| Emner | Protein folding
Science |
| Dewey |
