SPECTROSCOPY OF HEAVY ATOM PERTURBED BIOPOLYMERS

蛋白质-核酸相互作用在细胞内起重要作用， 过程和哺乳动物逆转录病毒的功能。 研究 这些相互作用，芳族残基的三重态将是 研究使用磷光和光学检测的磁性 共振（ODMR）。 同种异型蛋白将掺入色氨酸、苯丙氨酸和酪氨酸 可以在核酸中的红边选择性激发的类似物 配合物重要的是揭示影响 核酸结合的稳定性和序列选择性， 它们受芳族堆积影响的程度。 主 重点是HIV-1和SIV。 最重要的是研究 核衣壳（NC）蛋白与RNA基因组的相互作用 RNA的成熟。 NC蛋白的特征在于： 保守的Cys-X2-Cys-X4-His-X4-Cys逆转录病毒锌指基序 在特定位点含有芳香残基。 锌指已经 发现与模型RNA进行碱基堆积。 类似的互动 将被寻求。 RNA底物将延伸至含有以下的序列： psi，基因组RNA的腺苷酸化区。 自旋-晶格弛豫 三重态将被研究作为一个可能的报告 结构 诱导子和操纵子结合对单W 构建了E. colilac阻遏物的研究。 ODMR或 白细胞介素-1-β同种异体蛋白将用于测试Trp的作用 类似物掺入蛋白质结构。

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.