期刊论文详细信息
FEBS Letters | |
A novel method of preparing totally α‐deuterated amino acids for selective incorporation into proteins | |
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
【 预 览 】
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