RAMAN-SCATTERING OF COLLAGEN, GELATIN, AND ELASTIN
RAMAN-SCATTERING OF COLLAGEN, GELATIN, AND ELASTIN
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DOI：
10.1002/bip.1975.360140211
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发表时间：
1975-01-01
期刊：
影响因子：
2.9
通讯作者：
KOENIG, JL
中科院分区：
文献类型：
--
作者：
FRUSHOUR, BG;KOENIG, JL
给出了胶原蛋白、明胶和弹性蛋白的拉曼光谱。后两个光谱中的拉曼线是通过对明胶中的酰胺 N-H 基团进行氘化并通过研究组成氨基酸的叠加光谱来确定的。胶原蛋白和明胶光谱中 1271 和 1248 cm−1 处出现两条线，可归属于酰胺 III 模式。两条酰胺 III 线的出现可能与原胶原分子的双相性质有关，即沿链分布的富含脯氨酸（非极性）和贫脯氨酸（极性）区域。研究了水溶性小牛皮胶原蛋白中的熔化或胶原蛋白到明胶的转变，并将 1248-cm−1 酰胺 III 线分配给原胶原蛋白分子的 31 个螺旋区域。弹性蛋白被认为主要是随机的，拉曼光谱证实了这一说法。强酰胺 I 和 III 线分别出现在 1668 和 1254 cm−1 处，并且在 938 cm−1 处仅观察到弱散射。这些特征已被证明是蛋白质无序构象的特征。
The Raman spectra of collagen, gelatin, and elastin are presented. The Raman lines in the latter two spectra are assigned by deuterating the amide N‐H groups in gelatin and by studying the superposition spectra of the constituent amino acids. Two lines appear at 1271 and 1248 cm−1in the spectra of collagen and gelatin that can be assigned to the amide III mode. Possibly, the appearance of two amide III lines is related to the biphasic nature of the tropocollagen molecule, i.e., proline‐rich (nonpolar) and proline‐poor (polar) regions distributed along the chain. The melting, or collagen‐to‐gelatin transition, in water‐soluble calf skin collagen is studied and the 1248‐cm−1amide III line is assigned to the 31helical regions of the tropocollagen molecule.Elastin is thought to be mostly random and the Raman spectrum confirms this assertion. Strong amide I and III lines appear at 1668 and 1254 cm−1, respectively, and only weak scattering is observed at 938 cm−1. These features have been shown to be characteristic of the disordered conformation in proteins.