MTSL

MTSL

Names
IUPAC name S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl methanesulfonothioate
Other names MTSL
Identifiers
CAS Number	81213-52-7 Y
3D model (Jmol)	Interactive image
ChemSpider	117873 Y
PubChem	133628
InChI InChI=1S/C10H18NO3S2/c1-9(2)6-8(7-15-16(5,13)14)10(3,4)11(9)12/h6H,7H2,1-5H3 Y Key: BLSCGBLQCTWVPO-UHFFFAOYSA-N Y InChI=1/C10H18NO3S2/c1-9(2)6-8(7-15-16(5,13)14)10(3,4)11(9)12/h6H,7H2,1-5H3 Key: BLSCGBLQCTWVPO-UHFFFAOYAW
SMILES CC1(C=C(C(N1[O])(C)C)CSS(=O)(=O)C)C
Properties
Chemical formula	C10H18NO3S2
Molar mass	264.38 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

MTSL (S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl methanesulfonothioate) is a chemical compound which can be used as an amine oxide paramagnetic spin label in protein Electron paramagnetic resonance and nuclear magnetic resonance spectroscopy experiments. MTSL is attached via a disulfide bond to a cysteine residue, enabling site-directed spin labelling. Following attachment, which involves a Sulfinic acid (CH₃SO₂) leaving group,^[1][2] the MTSL moiety will add 184.3 daltons to the mass of the protein or peptide to which it is attached. The cysteine can be introduced using site-directed mutagenesis, and hence most positions in a protein can be labelled.

In Nuclear magnetic resonance the introduction of the paramagnetic group increases the relaxation rate of nearby nuclei. This can be detected as peak broadening and loss of intensity in peaks corresponding to nearby nuclei. Hence proximity can be inferred for all nuclei, that are affected. A major advantage of this method over traditional methods for obtaining distance restraints in protein NMR is the increased length, as paramagnetic relaxation enhancement can detect distances up to 25 Å (2.5 nm) as opposed to about 6 Å (0.6 nm) using the nuclear Overhauser effect. Spin labelling with MTSL is frequently used in investigation of residual structure in intrinsically unstructured proteins.

References

1. ↑ Kenyon, G.L. and Bruice, T.W. (1977). Novel sulfhydryl reagents. Methods In Enzymology 47, 407-430.
2. ↑ Berliner, L.J., Grunwald, J., Hankovszky, H.O., Hideg, K. (1982). A novel reversible thiol-specific spin label: papain active site labeling and inhibition. Analytical Biochemistry 119, 450-455.