Structual formation and structure-function relationship of protein studied with the use peptides

在生物系统中，蛋白质与彼此相互作用。在这项研究中，寡肽被用作蛋白质相互作用站点的模型，而蛋白质和肽之间的相互作用被研究在细节中。以下的结果已获得：1.细胞色素c（细胞c）被含有酪氨酸的肽、酪氨酸（TyrTyrPhe）降低，pH值为6.0-8.0。细胞C在高肽浓度下减少了，但在低浓度下反应并不有效。reciprocal initial rate constant （1/k_<int>） increased linearly against the reciprocal peptide concentration and against the linear proton concentration， whereas log k_<int>decreased linearly against the root of the ionic strength。这些结果显示了分离（TyrTyrPhe）。在一个酪氨酸位点上预先分解，减少细胞c由一个电静态复合体的形成。来自MALDI-TOF MS的反应产品的特性，从细胞c和YYF之间的反应中获得，形成一个 ... More 五角大楼和肽的其他酪氨酸衍生物得到了支持。这些产品应该是由酪氨酸基制成的。The results are interpreted that a cyt c_<ox>/（TyrTyrPhe）[tutomer] cyt c_<red>/（TyrTyrPhe）· equilibrium is formed， which is usually shifted to the left。这一等价物可能会改变产生的酪氨酸基基分子对不反应的TvrTvrPhe肽的反应的权利。Oxidized plastocyanin （PC） was reduced with TyrTyr at neutral pH. The reciprocal initial rate constant （1/k_<int>） increased linearly with the reciprocal TyrTyr concentration and proton concentration。结果显示，PC被TyrTyrTyr的分离物种减少了。A linear increase of log k_<int>with increase in the ionic strength was observed due to decrease in the electrostatic repulsion in the negatively charged PC and deprotonated （TyrTyr）。These results show that a metalloprotein Could be reduced at neutral pH with a tyrosine-containing oligopeptide。Less（低）

In biosystems, proteins interact with each other. In this research, oligopeptides are used as models of the protein interacting site, and the interaction between the protein and the peptide is studied in detail. The following results are obtained.1. Cytochrome c(cyt c) was reduced by a tyrosine-containing peptide, tyrosyltyrosylphenylalanine (TyrTyrPhe), at pH 6.0-8.0. Cyt c was reduced at high peptide concentration, whereas the reaction did not occur effectively at low concentration. The reciprocal initial rate constant (1/k_<int>) increased linearly against the reciprocal peptide concentration and against the linear proton concentration, whereas log k_<int> decreased linearly against the root of the ionic strength. These results show that deprotonated (TyrTyrPhe)., presumably deprotonated at a tyrosine site, reduces cyt c by formation of an electrostatic complex.2. From the MALDI-TOF MS spectra of the reaction products obtained from the reaction between cyt c and YYF, formation of a … More quinone and other tyrosine derivatives of the peptide was supported. These products should have been produced from a tyrosyl radical. The results are interpreted that a cyt c_<ox>/(TyrTyrPhe)【tautomer】 cyt c_<red>/(TyrTyrPhe)・ equilibrium is formed, which is usually shifted to the left. This equilibrium may shift to the right by reaction of the produced tyrosyl radical with the tyrosine sites of unreacted TvrTvrPhe peptides.3. Oxidized plastocyanin (PC) was reduced with TyrTyrTyr at neutral pH. The reciprocal initial rate constant (1/k_<int>) increased linearly with the reciprocal TyrTyrTyr concentration and proton concentration. The results showed that PC was reduced by the deprotonated species of TyrTyrTyr. A linear increase of log k_<int> with increase in the ionic strength was observed due to decrease in the electrostatic repulsion between negatively charged PC and deprotonated (TyrTyrTyr).These results show that a metalloprotein could be reduced at neutral pH with a tyrosine-containing oligopeptide. Less