Vibrational CD studies of the solution conformation of simple alanyl peptides as a function of pH.
Vibrational CD studies of the solution conformation of simple alanyl peptides as a function of pH.
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简单丙氨酰肽溶液构象作为 pH 函数的振动 CD 研究。
DOI:
10.1002/bip.360281116
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发表时间:
1989
期刊:
影响因子:
2.9
通讯作者:
Nafie,LA
中科院分区:
文献类型:
--
作者:
Zuk,WM;Freedman,TB;Nafie,LA
The CH‐stretching vibrational CD (VCD) spectra of glycyl‐L‐alanine,L‐alanylglycine, andL‐alanyl‐L‐alanine have been studied at neutral, high, and low pH in D2O solution. The intense positive VCD band attributed to the CαH stretch of the alanyl residue in glycyl‐L‐alanine at neutral pH is absent inL‐alanylglycine. In contrast to the VCD spectra ofL‐alanine, the positive methine‐stretching VCD band in glycyl‐L‐alanine andL‐alanyl‐L‐alanine is still present at pH 2. Based on the ring current mechanism, the VCD spectra are consistent with the presence of a five‐membered CO … HN intramolecular hydrogen‐bonded ring between the C‐terminal carboxylate and peptide NH groups at neutral and high pH, and a seven‐membered COH … OC hydrogen‐bonded ring between the C‐terminal carboxyl OH and peptide CO groups at low pH. In the N‐terminal alanyl residue, the peptide CO group is hydrogen bonded to the NHtransto the methine bond. The CH‐stretching VCD spectra ofL‐alanyl‐L‐alanyl‐L‐alanine at neutral pH are consistent with two intramolecularly hydrogen‐bonded conformations for the central alanyl residue.