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 ;
3D model (JSmol)	Interactive image;
ChemSpider	117873 ;
PubChem CID	133628;
CompTox Dashboard (EPA)	DTXSID80230944 ;
	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 Key: BLSCGBLQCTWVPO-UHFFFAOYSA-N ; 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 an organosulfur compound that is used as a nitroxide spin label.[1] MTSL is bifunctional, consisting of the nitroxide and the thiosulfonate ester functional groups. The nitroxide label is sterically protected, so it is relatively unreactive.

Labeling

MTSL is attached to proteins by reaction with thiol groups. The reaction exploits standard reactivity of thiosulfate esters. Sulfinic acid (CH₃SO₂H) is the leaving group:

RSO₂S-nitroxide + protein-SH → protein-S-S-nitroxide + RSO₂H

The heterodisulfide bond to the cysteine residue is robust, enabling site-directed spin labelling.[2][3] 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.

Spectroscopy

In Nuclear magnetic resonance the introduction of the paramagnetic group increases the relaxation rate of nearby nuclei.[1] Its presence 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

Christian Altenbach, Kyoung-Joon Oh, René J. Trabanino, Kálmán Hideg, Wayne L. Hubbell "Estimation of Inter-Residue Distances in Spin Labeled Proteins at Physiological Temperatures: Experimental Strategies and Practical Limitations" Biochemistry, 2001, volume 40, pp 15471–15482. doi:10.1021/bi011544w
Kenyon, G.L. and Bruice, T.W. (1977). Novel sulfhydryl reagents. Methods In Enzymology 47, 407-430. doi:10.1016/0076-6879(77)47042-3
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. doi:10.1016/0003-2697(82)90612-1

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[Altenbach-1] Christian Altenbach, Kyoung-Joon Oh, René J. Trabanino, Kálmán Hideg, Wayne L. Hubbell "Estimation of Inter-Residue Distances in Spin Labeled Proteins at Physiological Temperatures: Experimental Strategies and Practical Limitations" Biochemistry, 2001, volume 40, pp 15471–15482. doi:10.1021/bi011544w

[2] Kenyon, G.L. and Bruice, T.W. (1977). Novel sulfhydryl reagents. Methods In Enzymology 47, 407-430. doi:10.1016/0076-6879(77)47042-3

[3] 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. doi:10.1016/0003-2697(82)90612-1