SPECTROSCOPY OF HEAVY ATOM PERTURBED BIOPOLYMERS

蛋白质-核酸相互作用在细胞内起着至关重要的作用 在哺乳动物逆转录病毒的过程和功能方面。学习 这些相互作用芳香族残基的三重态将是 利用磷光和光学检测磁体的研究 共振(ODMR)。同种异体蛋白将包括色氨酸、苯丙氨酸和酪氨酸 可选择性地在核酸的红边激发的类似物 复合体。重要的是揭示影响经济增长的因素 核酸结合的稳定性和序列选择性 它们受芳香堆积影响的程度。初级阶段 重点将是HIV-1和SIV。最重要的将是对 核衣壳蛋白与RNA基因组的相互作用 在RNA包埋过程中成熟。NC蛋白的特征是 保守的Cys-X2-Cys-X4-His-X4-Cys逆转录病毒锌指模体 在特定位置含有芳香族残留物的。锌指已经被 发现与模型RNA进行碱基堆叠。类似的互动 都会被追捕。RNA底物将扩展到包含以下内容的序列 PSI，基因组RNA的包膜区。自旋-晶格弛豫 将作为可能的报告者来研究三重态 结构。诱导剂和操纵子结合对单W的影响 我们将研究大肠杆菌乳胶抑制子的结构。ODMR或 白介素1-β同种异体蛋白将用于测试色氨酸的效果 蛋白质结构上的类似物掺入。

Protein-nucleic acid interactions play essential roles in cellular processes and in the functioning of mammalian retroviruses. To study these interactions the triplet states of aromatic residues will be studied using phosphorescence and optical detection of magnetic resonance (ODMR). Alloproteins will incorporate Trp, Phe, and Tyr analogs that can be selectively excited at the red edge in nucleic acid complexes. Of importance is uncovering factors that influence the stability and sequence selectivity of nucleic acid binding and the extent to which they are influenced by aromatic stacking. The primary focus will be HIV-1 and SIV. Foremost will be studies of the interactions of nucleocapsid (NC) proteins with the RNA genome during maturation in RNA encapsidation. The NC proteins are characterized by conserved Cys-X2-Cys-X4-His-X4-Cys retroviral zinc finger motifs containing aromatic residues at specific sites. Zinc fingers have been found to undergo base-stacking with model RNAs. Similar interactions will be sought. RNA substrates will be extended to sequences containing psi, the encapsidation region of genomic RNA. Spin-lattice relaxation of the triplet state will be studied as a possible reporter of structure. Effects of inducer and operator binding on single-W constructs of E. coli lac repressor will be studied. ODMR or interleukin-1-beta alloproteins will be used to test effects of Trp analog incorporation on protein structure.