Novel conformationally-constrained beta-peptides characterized by 1H NMR chemical shifts.
Novel conformationally-constrained beta-peptides characterized by 1H NMR chemical shifts.
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DOI：
10.1039/b309584c
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发表时间：
2003-10
影响因子：
4.9
通讯作者：
R. J. Doerksen;Bin Chen;Jingkun Yuan;J. Winkler;M. Klein
中科院分区：
文献类型：
--
作者：
R. J. Doerksen;Bin Chen;Jingkun Yuan;J. Winkler;M. Klein
For a novel family of oxanorbornene beta-peptides, density functional theory computations of the three-dimensional structure and 1H NMR chemical shifts predict that the dimer and trimer form consecutive 8-membered hydrogen-bonded ring helices, which is supported by excellent agreement with experimental solution NMR data.
