Conformational Study of Solid Polypeptides by 1H Combined Rotation and Multiple Pulse Spectroscopy NMR
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- 作者：Akira Shoji ; Hideaki Kimura ; Takuo Ozaki ; Hisashi Sugisawa ; and Kenzo Deguchi
- 刊名：Journal of the American Chemical Society
- 出版年：1996
- 出版时间：August 14, 1996
- 年：1996
- 卷：118
- 期：32
- 页码：7604 - 7607
- 全文大小：117K
- 年卷期：v.118,no.32(August 14, 1996)
- ISSN：1520-5126
文摘
The relation between the 1H chemical shift and theconformation of linear homopolypeptides and cyclicdipeptides in the solid state has been studied utilizing the1H combined rotation and multiple pulsespectroscopy(CRAMPS) NMR method. It was found that the 1H chemicalshift of the H
signal of homopolypeptidesdependson the secondary structure such as -helix or 
-sheet form, whereasthose of the side-chain proton signals (H,H
,H
, etc.) are almost independent of the secondarystructure. The 1H chemical shifts of theH signal ofhomopolypeptides having the -helix and the -sheet forms were3.9-4.0 ppm and 5.1-5.5 ppm, respectively.Accordingly, the 1H chemical shift of theH is very useful for conformational analysis ofpolypeptides in the solidstate. Furthermore, it is shown that the 1H chemicalshift of the H and the NH signals of cyclic dipeptidesaresensitive to the ring conformation and the hydrogen bond length in thesolid state.
signal of homopolypeptidesdependson the secondary structure such as -helix or -sheet form, whereasthose of the side-chain proton signals (H,H,H, etc.) are almost independent of the secondarystructure. The 1H chemical shifts of theH signal ofhomopolypeptides having the -helix and the -sheet forms were3.9-4.0 ppm and 5.1-5.5 ppm, respectively.Accordingly, the 1H chemical shift of theH is very useful for conformational analysis ofpolypeptides in the solidstate. Furthermore, it is shown that the 1H chemicalshift of the H and the NH signals of cyclic dipeptidesaresensitive to the ring conformation and the hydrogen bond length in thesolid state.