UNIQUELY LABELED AMINO ACIDS FOR PROTEIN NMR

了解蛋白质折叠的方式和原因以及赋予独特的稳定折叠结构所需的相互作用的性质仍然是结构生物化学的中心目标。本提案中描述的研究旨在阐明稳定折叠和部分折叠蛋白质结构域所需的最小相互作用集。固态NMR将用于研究几种标记的氨基酸类似物的几何结构，这些氨基酸类似物可以作为氨基酸之间低势垒氢键（LBHB）的模型。高场溶液NMR将用于研究一种新的氢键网络在稳定外围亚基结合结构域的结构中所起的作用，外围亚基结合结构域是能够采用稳定，紧凑折叠的蛋白质的最小例子之一。NMR也将用于研究修饰的核糖体蛋白LP的结构。这些研究将有助于阐明稳定蛋白质折叠和部分折叠状态所需的相互作用。

An understanding of how and why proteins fold and of the nature of the interactions required to confer a unique stable folded structure remains a central objective of structural biochemistry The research described in this proposal is aimed at elucidating the minimum set of interactions required to stabilize folded and partially folded protein domains. Solid state NMR will be used to study the geometry in several labeled amino acid analogs that can serve as models for low barrier hydrogen bonds (LBHBs) between amino acids. High field solution NMR will be used to study the role a novel hydrogen-bonded network plays in stabilizing the structure of the peripheral subunit-binding domain, one of the smallest examples of a protein that is able to adopt a stable, compact fold. NMR will also be used to study the structure of a modified ribosomal protein, LP. These studies will help to elucidate the interactions required to stabilize folded and partially folded states of proteins.