Ultrafast Processing in Proteins and Other Assemblies

跨膜(TM)螺旋蛋白质结构随时间变化的残基水平可视化，快速 通过二维红外光谱分析可以发现折叠蛋白质和二级结构元素 (2D IR)一种新的、强大的结构生物学方法。多肽和蛋白质的同位素标记增强了 2D IR的空间分辨率，并将其扩展到更大的肽。螺旋-螺旋界面处涉及的弱键 将访问血糖素A的TM区段以获得界面区域中基团的运动和 了解它们如何稳定TM蛋白质中的螺旋-螺旋相互作用。2D IR揭示了以下方面的血脂波动 跨膜的空间排列。疏水效应、极性、氢键和氢键的2D IR 埋在地下的残基之间的其他弱相互作用启发了螺旋的机制和结构基础 协会。具有多个红外频率的2D IR，访问疏水界面，相关性 不同空间位置的波动与跨膜螺旋的N-H/N-D交换之间的关系。 独立折叠的蛋白质亚域是解决折叠问题的重要工具。FAST启用2D IR 非指数文件夹将允许访问二级结构的实时演变，并挑战所有 肌动蛋白结合蛋白的绒毛蛋白头盔的原子分子动力学，这与 肠道和肾脏的上皮组织。折叠途径将通过同位素标记的2D IR进行访问 螺旋和疏水核心。氧化还原蛋白中的中间产物细胞色素-c将是 用新的温度引起的pH跳跃进行了检验。对设计的多肽折叠的描述将是 2D IR寻求可视化它们如何组合并加强与理论的关系。这项研究涉及 膜蛋白是细胞生理学的重要组成部分：它们包括细胞表面受体、离子 通道、转运蛋白和氧化还原蛋白。完整的膜蛋白占总蛋白的近四分之一。 高等生物体中的编码序列，超过一半的商业药物针对这类 蛋白质。尽管如此，对它们的3D结构和动力学的研究仍然有限。蛋白质折叠是 高度相关，因为它是将遗传信息转化为所有生物功能的关键步骤 因此，对其进行控制是了解人类健康的重要组成部分。*

A residue level visualization of how protein structures change with time for transmembrane (TM) helices, fast folding proteins and elements of secondary structure will be found by two dimensional infrared spectroscopy (2D IR) a new, powerful method of structural biology. Isotopic labeling of peptides and proteins enhances the spatial resolution of 2D IR and extends it to larger peptides. Weak bonds involved at the helix-helix interfaces of TM sections of Glycophorin A will be accessed to obtain the motions of groups in the interface regions and discover how they stabilize helix-helix interactions in TM proteins. 2D IR exposes lipid fluctuations in terms of spatial arrangements across the membrane. 2D IR of hydrophobic effects, polarity, hydrogen bonding and other weak interactions between buried residues enlighten the mechanisms and structural basis of helix association. The 2D IR with multiple IR frequencies, accesses the hydrophobic interface, correlations between fluctuations at different spatial locations and the N-H/N-D exchange in transmembrane helices. Protein subdomains that fold independently are important tools for solving the folding problem. 2D IR on fast non-exponential folders will permit access to the real time evolution of secondary structure and challenge all atom molecular dynamics of the villin headpiece from the actin-bundling protein villin, which is implicated in the epithelium of the gut and kidney. The folding pathway will be accessed by 2D IR of isotope labeled helices and hydrophobic core. On-pathway intermediates in the redox protein, cytochrome-c, will be examined with novel temperature induced pH jumps. A description of the folding of designed peptides will be sought by 2D IR to visualize how they assemble and strengthen relations to theory. The research involves membrane proteins which are vital components of the cell physiology: they include cell-surface receptors, ion channels, transporters and redox proteins. Integral membrane proteins account for nearly one-quarter of all coding sequences in higher organisms, and more than half of all commercial drugs target this class of proteins. Despite this, study of their 3D structures and their dynamics remains limited. Protein folding is highly relevant because it is a key step in the conversion of genetic information into biological function of all types and therefore its control is an essential part of understanding human health. *