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Cover Picture: Synthesis of a 13 C‐Methyl‐Group‐Labeled Methionine Precursor as a Useful Tool for Simplifying Protein Structural Analysis by NMR Spectroscopy (ChemBioChem 6/2007)
Author(s) -
Fischer Michael,
Kloiber Karin,
Häusler Johannes,
Ledolter Karin,
Konrat Robert,
Schmid Walther
Publication year - 2007
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200790013
Subject(s) - heteronuclear single quantum coherence spectroscopy , methionine , chemistry , nuclear magnetic resonance spectroscopy , stereochemistry , amino acid , biochemistry
The cover picture shows the structure of the C‐terminal SH2 domain of the signal transduction protein PLC‐γ1. [4‐ 13 C]methylthio‐2‐oxobutanoates were used as precursors to introduce labeled methionines into the protein selectively. Synthesis of the labeled precursor was performed on a preparative scale by following a specially designed short and economical reaction sequence. Incorporation of the target protein into the SH2 domain was achieved by protein expression in E. coli BL21 (DE3) and confirmed by 13 C, 1 H HSQC spectroscopy. The presence of selectively labeled methionine S ‐methyl groups in defined positions significantly facilitates structural and dynamic NMR analysis of the protein. Since this synthetic route could give access to a variety of labeling patterns within the carbon skeleton of methionine, the precursor is a powerful tool for answering structural biological questions. Further details on the synthesis, incorporation and NMR investigations can be found in the article by R. Konrat, W. Schmid, et al. on p. 610 ff. The cover picture was drawn by using MOLMOL.