Since cysteine redox proteoforms (i) are virtually unstudied, we derived novel insights by computationally analysing the human proteome. Our analysis revealed a vast, effectively infinite, theoretical i space housing 3.02 x 10e169 unique cysteine redox proteoforms. For over 80% and 99% of the human proteome, the i space comprises 6.83 x 10e8 and 1.76 x 10e31 unique proteoforms, respectively. The heterogenous distribution of the i space by gene ontology terms, suggests, but does not prove, functional speciation. To theoretically limit the number of cysteine redox proteoforms that can be downloaded from the abstract i cloud, we implement novel equations. Protein copy numbers limit the i space by 161-logs to 4.04 x 10e7 unique cysteine redox proteoforms per HeLa cell. An immutable law: the number of cysteine redox proteoform molecules (Ni) must equal the number of cysteine-containing protein molecules. We compute an Ni value of 1.70 x 10e9 per HeLa cell. While Ni will be displaced from thermodynamic equilibrium towards the reduced state (e.g., 90%-reduced), it is possible that the number of partially oxidised cysteine redox proteoform molecules is in the order of 10e6-8 per HeLa cell. Consistent with this, 100%-oxidised forms were observed in 60% of the proteins studied to date. Our analysis advances understanding of redox biology at the proteoform level.