MERCURY TRANSPORT PROTEINS OF BACTERIAL MERCURY DETOXIFICATION SYSTEM

丝状菌上展示的多肽结构 噬菌体病毒颗粒可以作为表位和 蛋白质的独立折叠单位。多肽的荷尔蒙功能 或其他类型的效应器，当它们结合可溶性或膜结合时 感受器。当它们与抗体结合时，它们也充当表位。 多肽序列基本上有两个来源。多肽可以是 选自可通过生物方法制备的文库， 特别是噬菌体展示，或通过各种合成策略。 该文库的目的是生成所有可能的多肽 然后根据以下条件选择感兴趣的一个或几个 它们与靶分子的结合亲和力 受体蛋白。外壳蛋白的N-末端区域提供 如图所示，有利于稳定多肽构象的环境 由于插入的氨基酸序列的生物活性增加 进入外壳蛋白而不是游离肽。固态核磁共振 噬菌体上展示的几个表位的光谱给出了直接的 多肽结构折叠的证据。15N化学位移 酰胺的各向异性(CSA)和15N-1H偶极耦合测量 这些多肽的骨架部位表明这些多肽是 固定在病毒颗粒上，并提供了 他们的褶皱。主要抗原肽12个残基的表位分析 人类疟疾孢子体的决定因素被发现折叠成 三个转弯。HIV-1V3环6个残基表位被发现是 在噬菌体颗粒上流动。HIV-1抗体与此结合 展示在噬菌体上的表位导致了一种静止的折叠结构。

The structure of peptides displayed on the filamentous bacteriophage virus particles can be studied as epitopes and independent folding units of proteins. Peptides function as hormones or other types of effectors when they bind soluble or membrane bound receptors. They also act as epitopes when they bind to antibodies. There are basically two sources of peptide sequences. Peptides can be selected from libraries, which can be prepared by biological methods, in particular phage display , or by a variety of synthetic strategies. The purpose of the library is to generate all of the possible peptides of interest, and then to select the one or few of interest based on their binding affinity for a target molecule such as an antibody or receptor protein. The N-terminal region of the coat protein provides an environment conducive to stabilizing peptide conformation, as shown by the increased biological activity of amino acid sequences inserted into the coat protein versus the free peptide. Solid-state NMR spectra of several epitopes displayed on the phage gave direct evidence of the structural fold of the peptides. 15N chemical shift anisotropy (CSA) and 15N-1H dipolar coupling measurements of the amide backbone sites of these peptides indicate that the peptides are immobilized on the virus particle and provide structural details of their fold. Epitopes of a 12 residue peptide from the main antigenic determinant of the human malaria sporozite were found to fold into three turns. The 6 residue epitope of HIV-1 V3 loop was found to be mobile on the phage particle. Binding of an HIV-1 antibody to this epitope displayed on phage resulted in an immobile folded structure.