Schiller P W, Natarajan S, Bodanszky M
Int J Pept Protein Res. 1978 Sep;12(3):139-42. doi: 10.1111/j.1399-3011.1978.tb02877.x.
The solution conformation of a 7-peptide with the C-terminal sequence of cholecystokinin was investigated by evaluation of intramolecular resonance energy transfer between tyrosine (donor) in position 1 and tryptophan (acceptor) in position 4. From the relative enhancement of acceptor fluorescence a transfer efficiency of 0.70 +/- 0.04 was determined. The use of this parameter in Förster's equation permitted the calculation of the average intramolecular tyrosine-tryptophan separation, whereby the assumption of random donor-acceptor orientation was made. The resulting average distance of 10.0 +/- 0.3 A suggests some type of a folded conformation and excludes the existence of a fully extended chain in the N-terminal part of the peptide. A comparison with tyrosine-tryptophan distances observed in other biologically active polypeptides is made.
通过评估1位酪氨酸（供体）与4位色氨酸（受体）之间的分子内共振能量转移，研究了具有胆囊收缩素C端序列的七肽的溶液构象。根据受体荧光的相对增强，确定转移效率为0.70±0.04。在福斯特方程中使用该参数可以计算分子内酪氨酸-色氨酸的平均间距，其中假设供体-受体取向是随机的。所得平均距离为10.0±0.3 Å，表明存在某种折叠构象，并排除了该肽N端部分存在完全伸展链的可能性。还与其他生物活性多肽中观察到的酪氨酸-色氨酸距离进行了比较。
