STRUCTURE & EVOLUTION OF PLANT PHOTORECEPTOR PHYTOCHROME

分子动力学（CHARMM）技术被提议用于研究 两亲性肽在膜中的掺入， 这些肽相对于膜/水的取向 界面，以及这些环境中肽的构象。 本研究将使用两种膜模拟物。 一种是双相的 一种是水/四氯化碳模型，另一种是钠离子形成的胶束 十二烷基硫酸盐（SDS）。 两个系列的小神经肽， 包含初级两亲性的时刻，将用于这项工作。 的 这项工作的目标是比较合并的结果， 肽的取向（相对于膜/水 界面），并将MD与联合收割机 在这些介质中的模拟与NMR距离的限制，从 这些肽在SDS胶束中的NMR以确定 在相同的膜模拟环境中的肽。 分子 动力学（CHARMM）技术的研究提出了 两亲性肽在膜中的掺入， 这些肽相对于膜/水界面， 在这些环境中的肽构象。 两个膜 模拟物将用于本研究。 一个是双相模型， 十二烷基硫酸钠形成的胶束 （SDS）。 两个系列的小神经肽，其中包含初级 两亲性的时刻，将用于这项工作。 这方面的目标 工作是比较结果的纳入和定位 的肽（相对于膜/水界面）， 这两个膜模拟，并结合联合收割机的MD模拟在这些 介质与NMR距离的限制，从这些NMR获得 肽在SDS胶束中，以确定肽的构象 在相同的膜模拟环境中。

Molecular dynamics (CHARMM) techniques are proposed for the study of the incorporation of amphiphilic peptides in membrane, the orientation of these peptides with respect to the membrane/water interface, and the conformation of the peptides in these environments. Two membrane mimics will be used for this study. One is a biphasic model of water/CC14, the other is micelles formed by sodium dodecylsulfate (SDS). Two series of small neuropeptides, which contain primary amphiphilic moments, will be used for this work. The goals fo this work are to compare the results on the incorporation and orientation of the peptides (with respect to the membrane/water interface) in these two membrane mimics and to combine the MD simulation in these media with NMR distance constraints obtained from NMR of these peptides in SDS micelles to determine the conformation of the peptides in the same membrane mimic environment. Molecular dynamics (CHARMM) techniques are proposed for the study of the incorporation of amphiphilic peptides in membrane, the orientation of these peptides with respect to the membrane/water interface, and the conformation of the peptides in these environments. Two membrane mimics will be used for this study. One is a biphasic model of water/CC14, the other is micelles formed by sodium dodecylsulfate (SDS). Two series of small neuropeptides, which contain primary amphiphilic moments, will be used for this work. The goals for this work are to compare the results on the incorporation and orientation of the peptides (with respect to the membrane/water interface) in these two membrane mimics and to combine the MD simulation in these media with NMR distance constraints obtained from NMR of these peptides in SDS micelles to determine the conformation of the peptides in the same membrane mimic environment.