サービス品質の管理・評価の課題

departmental bulletin pape

都道府県ごとの調査状況の違いは回答者の属性および回答結果に影響を与えるか : マルチレベルモデルを用いた検討

「住民の意識調査に関する有識者研究委員会」では、日本社会の体感治安を測定する標準的な調査手法を開発するために、2015年7～9月、全国の都道府県警の主導のもと、免許更新のために運転免許試験場・センターおよび警察署を訪れた一般市民を対象に自記式質問紙調査を実施した。本稿では、46都道府県に属する42,768人から得られたデータを用いて、都道府県間の調査実施状況の違いが回答者の属性および回答に影響を及ぼしたかをマルチレベルモデルにより検討した。分析の結果から、都道府県レベルの試験場・センター回答者割合および違反区分回答者割合は、個人レベルの変数を調整したうえでなお、回答者の性別、年齢、警察への信頼と関連することが示された。一方、体感治安は都道府県レベルの調査実施状況とは関連しないことが示された。これらの結果から、日本社会の体感治安を測定するという本調査の主要な目的にとっては、今回提案された調査手法が有用であることが示唆された。 To develop a standard survey method for measuring the subjective security in Japanese sosiety, from July to September 2015, "the Study Committee for the Subjective Security Survey" conducted a self-administered questionnaire-based survey on the initiative of the prefectural police department, which targeted people who visited a Driver's License Center or police station for license renewal. This paper examined whether the differences in the survey situation among prefectures were associated with respondents' demographic characteristics and responses, using data from 42,768 respondents living in 46 prefectures. The results of multilevel analyses show that prefecture-level proportions of those who participated in the survey at a Driver's License Center and those who were in traffic violation class were associated with respondents' sex, age, and trust in the police. On the other hand, subjective security was not linked to prefecture-level variables. These results suggest that the proposed survey protocol is useful for meaturing subjective security in Japanese society.1. はじめに：「全国統一治安意識調査」におけるサンプリングをどのように考えるか 2. 方法：用いたデータおよび統計解析 3. 結果：都道府県レベル変数と回答者の属性・体感治安・警察への信頼の関連 4. 考察・まとめtextapplication/pdfdepartmental bulletin pape

Mild cognitive impairment in older adults with pre-dialysis patients with chronic kidney disease: Prevalence and association with physical function

application/pdfNephrology. 2019, 24 (1), P.50-55journal articl

A research on cooperative problem solving learning in mathematics education : construction learning processes and object of evaluation

departmental bulletin pape

Observation of B+→pp̅π+, B0→pp̅K0, and B+→pp̅K*+

journal articl

A NOTE ON COMMON FIXED POINTS

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A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact

VirB11 ATPases are hexameric assemblies that power type IV secretion systems in bacteria. The hexamer of Brucella suis VirB11 (BsB11), like that of the Helicobacter pylori VirB11 (Hp0525), consists of a double ring structure formed by the N-terminal and C-terminal domains of each monomer. However, the monomer differs dramatically from that of Hp0525 by a large domain swap that leaves the hexameric assembly intact but profoundly alters the nucleotide-binding site and the interface between subunits

Calorimetric and Structural Studies of 1,2,3-Trisubstituted Cyclopropanes as Conformationally Constrained Peptide Inhibitors of Src SH2 Domain Binding

Isothermal titration calorimetry and X-ray crystallography have been used to determine the structural and thermodynamic consequences associated with constraining the pTyr residue of the pYEEI ligand for the Src Homology 2 domain of the Src kinase (Src SH2 domain). The conformationally constrained peptide mimics that were used are cyclopropane-derived isosteres whereby a cyclopropane ring substitutes to the N-Cα-Cβ atoms of the phosphotyrosine. Comparison of the thermodynamic data for the binding of the conformationally constrained peptide mimics relative to their equivalent flexible analogues as well as a native tetrapeptide revealed an entropic advantage of 5−9 cal mol-1 K-1 for the binding of the conformationally constrained ligands. However, an unexpected drop in enthalpy for the binding of the conformationally constrained ligands relative to their flexible analogues was also observed. To evaluate whether these differences reflected conformational variations in peptide binding modes, we have determined the crystal structure of a complex of the Src SH2 domain bound to one of the conformationally constrained peptide mimics. Comparison of this new structure with that of the Src SH2 domain bound to a natural 11-mer peptide (Waksman et al. Cell 1993, 72, 779−790) revealed only very small differences. Hence, cyclopropane-derived peptides are excellent mimics of the bound state of their flexible analogues. However, a rigorous analysis of the structures and of the surface areas at the binding interface, and subsequent computational derivation of the energetic binding parameters, failed to predict the observed differences between the binding thermodynamics of the rigidified and flexible ligands, suggesting that the drop in enthalpy observed with the conformationally constrained peptide mimic arises from sources other than changes in buried surface areas, though the exact origin of the differences remains unclear

Calorimetric and Structural Studies of 1,2,3-Trisubstituted Cyclopropanes as Conformationally Constrained Peptide Inhibitors of Src SH2 Domain Binding

Isothermal titration calorimetry and X-ray crystallography have been used to determine the structural and thermodynamic consequences associated with constraining the pTyr residue of the pYEEI ligand for the Src Homology 2 domain of the Src kinase (Src SH2 domain). The conformationally constrained peptide mimics that were used are cyclopropane-derived isosteres whereby a cyclopropane ring substitutes to the N-Cα-Cβ atoms of the phosphotyrosine. Comparison of the thermodynamic data for the binding of the conformationally constrained peptide mimics relative to their equivalent flexible analogues as well as a native tetrapeptide revealed an entropic advantage of 5−9 cal mol-1 K-1 for the binding of the conformationally constrained ligands. However, an unexpected drop in enthalpy for the binding of the conformationally constrained ligands relative to their flexible analogues was also observed. To evaluate whether these differences reflected conformational variations in peptide binding modes, we have determined the crystal structure of a complex of the Src SH2 domain bound to one of the conformationally constrained peptide mimics. Comparison of this new structure with that of the Src SH2 domain bound to a natural 11-mer peptide (Waksman et al. Cell 1993, 72, 779−790) revealed only very small differences. Hence, cyclopropane-derived peptides are excellent mimics of the bound state of their flexible analogues. However, a rigorous analysis of the structures and of the surface areas at the binding interface, and subsequent computational derivation of the energetic binding parameters, failed to predict the observed differences between the binding thermodynamics of the rigidified and flexible ligands, suggesting that the drop in enthalpy observed with the conformationally constrained peptide mimic arises from sources other than changes in buried surface areas, though the exact origin of the differences remains unclear

Rapid, Accurate, and Precise Calculation of Relative Binding Affinities for the SH2 Domain Using a Computational Grid

We describe and apply a method that reduces the time taken to calculate binding free energies using thermodynamic integration. This method uses a stack of grid software, which we call STIMD, that allows the scientist to easily distribute the necessary simulations around a computational grid thereby accelerating the process. We use this method to study how a series of phosphopeptides binds to the Src SH2 domain. The binding of phosphopeptides to the Src SH2 domain is described by the “two-pronged plug two-holed socket” model, and we investigate this model by reducing the length of the aliphatic side chain that engages the second of the two sockets through two successive alchemical mutations. Seven different values of ΔΔG have been calculated, and we report good agreement with experiment. We then propose an extension to this model using the insights gained from a free energy component analysis