Weber J, Rösch P, Adermann K, Forssmann W G, Wokaun A
Lehrstuhl für Struktur und Chemie der Biopolymere, Universität Bayreuth, Germany.
Biochim Biophys Acta. 1994 Aug 17;1207(2):231-5. doi: 10.1016/0167-4838(94)00040-9.
The recently discovered 32 amino-acid natriuretic peptide urodilatin was chemically synthesized and subjected to two-dimensional proton nuclear magnetic resonance (NMR) spectroscopy studies in aqueous solution in order to determine the structural state of urodilatin. In contrast to earlier studies on very closely related peptides, such as cardiodilatin (CDD/ANP-99-126) and brain natriuretic peptide (BNP), spectra of urodilatin were extremely well resolved even in millimolar concentration in H2O so that the complete sequence specific resonance assignments could be achieved. No long range NOEs could be detected, except between residues close to the single cystine bond. This leads to the conclusion that urodilatin in aqueous solution is a random coil peptide with the exception of the region around the cystine bond.
最近发现的由32个氨基酸组成的利钠肽尿舒张素经化学合成，并在水溶液中进行了二维质子核磁共振（NMR）光谱研究，以确定尿舒张素的结构状态。与早期对密切相关肽的研究不同，如心钠素（CDD/ANP-99-126）和脑钠肽（BNP），即使在H2O中毫摩尔浓度下，尿舒张素的光谱也能得到极好的解析，从而可以实现完整的序列特异性共振归属。除了靠近单个胱氨酸键的残基之间，未检测到长程核Overhauser效应（NOE）。这导致得出结论，除了胱氨酸键周围的区域外，水溶液中的尿舒张素是一种无规卷曲肽。
