摘要
报导了粉末状结晶[des His^(35),des Gly^(40)]γ-TGF-α(34—43)的拉曼光谱。酰胺Ⅰ振动谱带在1669cm^(-1),酰胺Ⅲ振动谱带在1337、1262和1242 cm^(-1),硫—硫键的振动谱带在504cm^(-1),酪氨酸残基的特征谱带在847、830和642 cm^(-1)。它们定性地证明了肽链可能由β-回转和β-折叠织成,酪氨酸残基在肽链中呈全“暴露”式,硫—硫键部位的几何构型为扭式-扭式-扭式。据此提出了该肽链的结构模型。
The Raman Spectra of the powdered crystalline of (des His^(35), des Gly^(40)) γ-TGF-α(34—43) have been studied. The amide Ⅰ band appears at 1669cm^(-1), amide Ⅲ band appears at 1337, 1262 and 1242cm^(-1). The characteristic Raman bands of the tyrosine residue are at 847,830 and 642cm^(-1). The band of the S—S bond is at 504cm^(-1). All the characteristic Raman bands of this peptide prove that its structure consists of the β-turn and β-sheet. The tyrosine residue is 'exposed' and the conformation of the rarbon atoms in the disulfide bridge C—C—S—S—C—C is gauche-gauche-gauche. A Space model of this peptide has been presented on the basis of the Raman data.
出处
《光谱学与光谱分析》
SCIE
EI
CAS
CSCD
北大核心
1990年第1期24-26,共3页
Spectroscopy and Spectral Analysis
基金
国家自然科学基金
