Evidence for tertiary structure in aqueous solutions of human beta-endorphin as shown by difference absorption spectroscopy.
Evidence for tertiary structure in aqueous solutions of human beta-endorphin as shown by difference absorption spectroscopy.
复制标题
差异吸收光谱显示人 β-内啡肽水溶液中三级结构的证据。
作者：
Bewley,TA;Li,CH
托马斯A. Bewley* 和Choh Hao Li摘要：人0-内啡肽水溶液中存在明显的三级结构，这一点已被该激素和合成类似物的嗜热菌蛋白酶的差异吸收光谱所证实。结果表明，Tyr 1 *、Lys 28的-氨基以及Thr 6 * 和Ser 10之间的一些残基参与形成和稳定分子的折叠形式。虽然对应于人0-内啡肽的前9个残基的肽显示出三级结构的明确证据，但五肽甲硫氨酸-脑啡肽却没有。脑啡肽（EK）1和内啡肽（EP）是重要的、天然存在的动物源性阿片肽。EK是含有NH 2-末端酪氨酸的五肽（Hughes等人，1975年）。EP较大，并且包含NH 2末端前5个残基的EK序列（Li，1981）。CD研究表明，构象可能在EP的生物活性中起一定作用（Li，1981）。f来自加州大学激素研究实验室，弗朗西斯科，加州94143。1982年10月22日收到。这项工作得到了美国国立卫生研究院（AM-18677和GM-2907）和美国国立精神卫生研究院（MH-30245）的赠款。
Thomas A. Bewley* and Choh Hao Li abstract: The presence of a distinct tertiary structure in aqueous solutions of human 0-endorphin has beendemon-strated by difference absorption spectroscopy of thermolysin digests of the hormone and synthetic analogues. The results demonstrate that the-amino group of Tyr1****, Lys28, and some residue (s) between Thr6*** and Ser10 are involved in forming and stabilizing the folded form of the molecule. Although a peptide corresponding to the first nine residues of human 0-endorphin shows definite evidence of tertiarystructure, the pentapeptide methionine-enkephalin does not. e enkephalins (EK) 1 and endorphins (EP) are important, naturally occurring opioidpeptides of animal origin. EK’s are pentapeptides containing an NH2-terminal tyrosine (Hughes et al., 1975). The EP’s are larger and contain an EK sequence for the first five residues from the NH2 terminus (Li, 1981). CD studies have suggested that conformation may play some role in the biological activities of EP (Li, 1981). f From the Hormone Research Laboratory, University of California, San Francisco, California 94143. Received October 22, 1982. This work was supported in part by grants from the National Institutes of Health (AM-18677 and GM-2907) and the National Institutes of Mental Health (MH-30245).