A novel method of preparing totally α‐deuterated amino acids for selective incorporation into proteins

FEBS Letters

Ostler, G.¹  Carr, M.D.¹  Birdsall, B.¹  Feeney, J.¹  Kairi, M.¹ 

[1] Laboratory of Molecular Structure, National Institute for Medical Research, Mill Hill, London NW7 1AA, UK

关键词: NMR;    2D;    Dihydrofolate reductase;    Selective deuteration;   

DOI  :  10.1016/0014-5793(90)80483-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The pyridoxal/²H₂O exchange reaction of the α-CH of amino acids is known to be accompanied by racemisation: Thus by using a D-amino acid as the starting material any L-amino acid formed in the reaction will be essentially fully deuterated at its α-position. We have used this method to prepare α-deuterated L-valine and incorporated this biosynthetically into L. casei dihydrofolate reductase. A comparison of the αCH-NH fingerprint regions of COSY spectra of deuterated and normal DHFR complexes allows one to identify cross-peaks from 15 of the 16 valine residues.

【 授权许可】

Unknown