Ernst-Fonberg M L, Worsham L M, Williams S G
Department of Biochemistry, James H. Quillen College of Medicine, East Tennessee State University, Johnson City 37614.
Biochim Biophys Acta. 1993 Aug 7;1164(3):273-82. doi: 10.1016/0167-4838(93)90259-t.
Protein solution structures were analyzed by horizontal attenuated total reflectance (ATR) FTIR spectroscopy. Secondary structure compositions determined from analyses of amide-I and II region and amide-III region difference spectra were compared. Data for proteins of known solution structure, cytochrome c, concanavalin A and lysozyme, were compared with those reported in the literature. Melittin, a peptide from bee venom whose secondary structural configuration varies depending upon solution conditions was also examined. Acyl-carrier protein (ACP) is a small protein of recognized dynamic structure that in its diverse physiologic roles interacts specifically with numerous different proteins. Horizontal ATR FTIR analysis of ACP's secondary structure indicated a predominantly helical structure best defined as a combination of ordered and disordered helices. The FTIR-derived structural composition agreed with those determined for ACP by other techniques. Comparison of independent analyses of the amide-I and III regions to determine protein configuration compositions was a useful method of verifying the internal consistency of the calculated structural compositions of dynamically-structured proteins.
通过水平衰减全反射（ATR）傅里叶变换红外光谱（FTIR）分析蛋白质溶液结构。比较了根据酰胺-I和II区域以及酰胺-III区域差光谱分析确定的二级结构组成。将已知溶液结构的蛋白质（细胞色素c、伴刀豆球蛋白A和溶菌酶）的数据与文献报道的数据进行了比较。还研究了蜂毒肽蜂毒素，其二级结构构型因溶液条件而异。酰基载体蛋白（ACP）是一种具有公认动态结构的小蛋白，在其多种生理作用中与许多不同的蛋白特异性相互作用。对ACP二级结构的水平ATR FTIR分析表明，其主要为螺旋结构，最好定义为有序螺旋和无序螺旋的组合。FTIR得出的结构组成与通过其他技术确定的ACP结构组成一致。通过比较酰胺-I和III区域的独立分析来确定蛋白质构型组成，是验证动态结构蛋白质计算结构组成内部一致性的一种有用方法。
