Random-coil chemical shifts of phosphorylated amino acids
Random-coil chemical shifts of phosphorylated amino acids
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DOI：
10.1023/a:1008375029746
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发表时间：
1999-11-01
影响因子：
2.7
通讯作者：
Lumb, KJ
中科院分区：
文献类型：
--
作者：
Bienkiewicz, EA;Lumb, KJ
在25 ℃水中，在pH 2 - 9范围内，获得了保护肽Ac-Gly-Gly-X-Gly-Gly-NH 2中磷酸化氨基酸pSer、pThr和pTyr的H-1、C-13、N-15和P-31无规卷曲化学位移和磷酸pK（a）值。ROESY光谱分析表明，肽是非结构化的。磷酸化诱导无规卷曲化学位移的变化，其中一些与二级结构形成引起的变化相当，因此在基于化学位移的结构分析中具有重要意义。
The H-1, C-13, N-15 and P-31 random-coil chemical shifts and phosphate pK(a) values of the phosphorylated amino acids pSer, pThr and pTyr in the protected peptide Ac-Gly-Gly-X-Gly-Gly-NH2 have been obtained in water at 25 degrees C over the pH range 2 to 9. Analysis of ROESY spectra indicates that the peptides are unstructured. Phosphorylation induces changes in random-coil chemical shifts, some of which are comparable to those caused by secondary structure formation, and are therefore significant in structural analyses based on the chemical shift.