ROLE OF AN AROMATIC AMINO ACID IN PROTEIN BINDING SITES

芳香氨基酸在蛋白质结合位点中的作用

• 批准号: 3438607
• 负责人: GERMAINE E GOGEL
• 金额: $ 6.81万
• 依托单位: COLGATE UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1988
• 资助国家: 美国
• 起止时间: 1988-06-01 至 1991-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3438607
• 关键词: Rhodospirillum; bacterial proteins; binding proteins; bioenergetics; chemical binding; chlorophyll; chromatophore; hydropathy; membrane permeability; membrane proteins; oxidation; peptide chemical synthesis; photosynthesis; protein engineering; protein sequence; reagent /indicator; tryptophan; ultraviolet spectrometry

Tryptophan is a hydrophobic, aromatic amino acid which serves important functions in enzyme active sites and in other protein binding sites. Many proteins bind large hydrophobic and aromatic molecules such as porphyrins, and tryptophan is involved in some of the binding sites. However, little detail concerning the molecular environment of the bound molecules in membrane proteins is available because crystal structures for most membrane proteins are not yet available. Chlorophyll binding proteins from bacteria are examples of such proteins. Chlorophyll binding proteins are responsible for capture and transfer of light energy in photosynthesis. The amino acid sequences of the proteins and rates of energy transfer are known, making them ideal candidates for characterization of the protein binding sites. By chemically modifying the aromatic amino acid tryptophan, we will alter these amino acids within the chlorophyll binding proteins. We will test whether the binding of chlorophyll and the activity of the protein in energy transfer have been changed. A spectrophotometric which will be used to detect changes in the binding of chlorophyll and to quantitate these changes will be purchased. In addition to chemical modification reactions and spectrophotometric assays, protein purification and qualification procedures will be used in this research. Chlorophyll binding proteins provide the environment required to promote energy transfer between different pigment molecules and ultimately to the photochemical reaction center, where the oxidation-reduction reactions of photosynthesis begin. By improving our understanding of how tryptophan functions in these proteins, we will improve our understanding of how these energy transfer processes occur with high efficiency in photosynthesis, as well as our general understanding of the role of hydrophobic binding sites in proteins.

色氨酸是一种疏水、芳香的氨基酸，它的作用是 酶活性部位和其他蛋白质的重要功能 结合部位。许多蛋白质结合了大量的疏水性和芳香性 像卟啉和色氨酸这样的分子参与了一些 结合位点数。然而，关于这一事件的细节很少 膜中结合分子的分子环境 蛋白质是可用的，因为大多数的晶体结构 膜蛋白目前还不可用。叶绿素结合 细菌中的蛋白质就是这种蛋白质的例子。叶绿素 结合蛋白负责捕获和传输光 光合作用中的能量。该基因的氨基酸序列 蛋白质和能量转移的速度是已知的，使它们 是表征蛋白质结合位点的理想候选者。 通过对芳香氨基酸色氨酸进行化学修饰，我们 会改变这些与叶绿素结合的氨基酸 蛋白质。我们将测试叶绿素和植物的结合是否 蛋白质在能量转移中的活性发生了变化。一个 分光光度法，将用于检测 结合叶绿素和量化这些变化将是 购买的。除了化学改性反应和 分光光度分析、蛋白质提纯和鉴定 程序将用于本研究。 叶绿素结合蛋白提供所需的环境 促进不同色素分子之间的能量转移 最终到达光化学反应中心，在那里 光合作用的氧化还原反应开始。通过 提高我们对色氨酸在这些细胞中的功能的理解 蛋白质，我们将提高我们对这些能量是如何 转移过程在光合作用中以高效率发生，如 以及我们对疏水的作用的一般理解 蛋白质中的结合部位。