Proteomics

Dataset Information

ScandiumIII


ABSTRACT: Recently, it has been reported that some metal complexes can act as artificial proteases. In particular, the Lewis acid scandium(III) triflate has been shown to catalyze the cleavage of peptide bonds N- and C-terminal to serine and threonine residues. Therefore, we investigated if this compound can also be used for the cleavage of proteins. For this purpose, several single proteins, the 20S immune-proteasome (17 proteins), and the Universal Proteomics Standard UPS1 (48 proteins) were analyzed by MALDI-MS and/or LC-MS. A high cleavage specificity N-terminal to serine and threonine residues was observed.

INSTRUMENT(S):

ORGANISM(S): Equus Caballus (horse) Homo Sapiens (human) Bos Taurus (bovine)

SUBMITTER: Christian Koehler  

LAB HEAD: Bernd Thiede

PROVIDER: PXD014918 | Pride | 2020-05-26

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
190104_Sc_A1AG_60C_1.dat Other
190104_Sc_A1AG_60C_1.mgf Mgf
190104_Sc_A1AG_60C_1.raw Raw
190104_Sc_CasB_60C_1.dat Other
190104_Sc_CasB_60C_1.mgf Mgf
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