STRUCTURE & EVOLUTION OF PLANT PHOTORECEPTOR PHYTOCHROME

分子动力学(CHARMM)技术被提出用于研究 在膜中掺入两亲性多肽， 这些多肽相对于膜/水的取向 界面，以及在这些环境中多肽的构象。 这项研究将使用两种膜模拟物。一种是双相 水/CC14模型，另一种是钠形成的胶束 十二烷基硫酸酯(十二烷基硫酸酯)。两个系列的小神经肽，它们 包含初级两亲性的瞬间，将被用于这项工作。这个 这项工作的目标是比较合并和 多肽的取向(相对于膜/水 界面)在这两种膜模拟物中并结合MD 在具有核磁共振距离约束的这些介质中进行模拟 这些多肽在十二烷基硫酸钠胶束中的核磁共振研究 同一膜中的多肽模拟环境。分子 动力学(CHARMM)技术被提出用于研究 两亲性多肽在膜中的掺入，膜的定向 这些多肽与膜/水界面有关，并且 多肽在这些环境中的构象。两层膜 这项研究将使用模仿法。一种是两相模型 水/CC14，另一种是十二烷基硫酸钠形成的胶束 (SDS)。两个系列的小神经肽，它们包含初级 两亲性的瞬间，将被用于这部作品。这样做的目标是 工作是比较合并和定向的结果 中的多肽(相对于膜/水界面) 这两种膜模拟并结合MD模拟在这些 由这些核磁共振获得的具有核磁共振距离约束的介质 在十二烷基硫酸钠胶束中测定多肽的构象 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.