Conformational Dynamics of Small Peptides

小肽的生物学重要性与它们在许多不同类型的受体上的活性有关。作为其环境函数的小线性多肽的构象灵活性要求对构象动力学有非常准确的理解，以便通过计算方法进行预测。这项工作将用含时红外光谱方法测量构象变化的活化能。多肽的N-H振动运动对几何构型变化和溶剂相互作用非常敏感。通过实验激发皮秒时间尺度上的大的温度跃变，多肽的构象重排和20纳秒以上红外N-H区随时间变化的实验测量可以与构象动力学有关。这些数据将使分子动力学模型的测试和改进成为可能。%这项工作的影响是能够对各种生物现象中的肽相互作用进行准确的计算预测。这种准确的预测对于理解结构和功能关系是必不可少的。

The biological importance of small peptides relates to their activity at receptor sites of many different types. The conformational flexibility of small linear peptides as a function of their environment requires a very accurate understanding of conformational dynamics in order to make predictions by computational methods. This project work will measure the activation energies for conformation changes by time dependent infrared spectroscopic methods. The N-H vibrational motion of peptides is very sensitive to geometric changes and solvent interactions. By experimentally exciting a large temperature jump on a picosecond time scale the peptide conformations rearrange and time dependent experimental measurements of the changes in the N-H region of the infrared over 20 nanoseconds can be related to conformational dynamics. The data will allow testing and refinement of molecular dynamics models. %%% The impact of this work is to enable accurate computational predictions of peptide interactions in a wide variety of biological phenomena. Such accurate predictions are essential to understand structure and function relationships.