Infrared spectroscopic discrimination between alpha- and 3(10)-helices in globular proteins. Reexamination of Amide I infrared bands of alpha-lactalbumin and their assignment to secondary structures.

S J Prestrelski, D M Byler, M P Thompson
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Abstract

We have undertaken a new and more detailed Fourier-transform infrared (FTIR) spectroscopic study of alpha-lactalbumin (in D2O solution) aimed at correlating its secondary structures to observed Amide I' infrared bands. The spectra reported here were interpreted in light of the recently determined crystal structure of alpha-lactalbumin and by comparison with the spectra and structure of the homologous protein lysozyme. Of particular importance is the new evidence supporting the assignment of the band at 1639 cm-1 to 3(10)-helices. This assignment is in excellent agreement with one based on theoretical and experimental studies of 3(10)-helical polypeptides. The frequency observed for 3(10)-helices is distinctly different from that at which alpha-helices are typically found (viz., around 1655 cm-1). In the present study, two bands are clearly resolved in the latter region at 1651 and 1659 cm-1. Both are apparently associated with alpha-helices. These results suggest that for D2O solutions of globular proteins. FTIR spectroscopy can be a facile method for detecting the presence of these two different types of helical conformation and distinguishing between them. This provides a distinct advantage over ultraviolet circular dichroism spectroscopy (UV-CD). This work also provides a basis for future studies of alpha-lactalbumin which examine the effects of environment (e.g., pH, temperature) and ligands (e.g., Ca2+, Mn2+) on its conformation.

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球形蛋白中α -和3(10)-螺旋的红外光谱区分。α -乳清蛋白酰胺I红外波段及其二级结构的重新研究。
我们对α -乳清蛋白(在D2O溶液中)进行了新的更详细的傅里叶变换红外光谱研究,旨在将其二级结构与观察到的酰胺I红外波段联系起来。本文报道的光谱是根据最近确定的α -乳白蛋白晶体结构,并与同源蛋白溶菌酶的光谱和结构进行比较来解释的。特别重要的是支持1639 cm-1到3(10)-螺旋波段分配的新证据。该作业与基于3(10)-螺旋多肽的理论和实验研究的作业非常一致。观测到的3(10)螺旋的频率明显不同于通常发现的α螺旋(即大约1655厘米-1)。在本研究中,后一区域在1651和1659 cm-1处清晰地分辨出两个波段。两者显然都与α螺旋有关。这些结果表明,对于D2O溶液的球状蛋白。FTIR光谱可以是一种简便的方法来检测这两种不同类型的螺旋构象的存在并区分它们。这提供了比紫外线圆二色光谱(UV-CD)明显的优势。这项工作也为α -乳清蛋白的未来研究提供了基础,研究环境(如pH,温度)和配体(如Ca2+, Mn2+)对其构象的影响。
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