VIBRATIONAL-SPECTRUM OF UNORDERED POLYPEPTIDE-CHAIN - RAMAN STUDY OF FEATHER KERATIN
VIBRATIONAL-SPECTRUM OF UNORDERED POLYPEPTIDE-CHAIN - RAMAN STUDY OF FEATHER KERATIN
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DOI：
10.1002/bip.1976.360150807
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发表时间：
1976-01-01
期刊：
影响因子：
2.9
通讯作者：
KRIMM, S
中科院分区：
文献类型：
--
作者：
HSU, SL;MOORE, WH;KRIMM, S
获得了天然羽毛角蛋白和溶解羽毛角蛋白的拉曼光谱，并用谱带分辨技术分析了酰胺I和酰胺III区域。天然形式的酰胺I区表明，至少%的蛋白质具有反平行链褶皱片状结构，其余的是无序的。对于溶解的角蛋白，所有的蛋白质都处于无序状态。酰胺III区不那么容易被分析成组成成分。对N-乙酰-L-丙氨酸-N-甲酰胺的简正振动分析支持酰胺Ⅲ区在表征无序结构方面不如酰胺I区的结论。即使在后一种情况下，也必须谨慎使用，因为观察到的酰胺I带是特定无序体系中构象分布的平均值。
Raman spectra of native and solubilized feather keratin [from Anas platyrhynchos] were obtained, and the amide I and amide III regions were analyzed by band resolution techniques. The amide I region of the native form indicates that at least 64% of the protein has an antiparallel chain pleated sheet structure, the remainder being unordered. For the solubilized keratin all of the protein is in an unordered state. The amide III region is not as easily analyzed into component contributions. Normal vibration analyses on N-acetyl-L-alanine-N-methylamide support the conclusion that the amide III region is not as satisfactory as the amide I region in characterizing unordered structures. Even in the latter case caution must be used, since the observed amide I band is an average over the conformational distribution in the particular unordered system.