Peran Gaya Kepemimpinan Transformasional Memoderasi Pengaruh Motivasi Intrinsik dan Kecerdasan Emosional terhadap Kinerja Guru (Studi Kasus pada SMA Negeri di Kecamatan Pati Kabupaten Pati)

This research is intended to examine the influence of motivation intrinsic and emotional intelligence to the state senior high school teachers\u27 work performance with the moderation of transformational leadership style. The specific purpose of this research is to examine the role of transformational leadership style moderates the influence of intrinsic motivation and emotional intelligence to the teachers\u27 work performance. The USAge of this research is to explain and expand the previous research about the role of transformational leadership style moderates the influence of intrinsic motivation and emotional intelligence to the teachers\u27 work performance. This research used the population of 116 teachers of state senior high school in Pati District, Pati Regency. The technique of sample collection used in this research is non-probability sampling with the purposive method. The analysis technique used in this research is regression model moderate quasi. Based on the research result can be conduded that: intrinsic motivation influences teachers\u27 work performance, emotional intelligence influences the teachers\u27 work performance, transformational leadership style do not moderate the influence of intrinsic motivation to teachers\u27 work performance, , transformational leadership style strengthen the influence of emotional intelligence to the teachers\u27 workperformance

The influence of mass media on countryside leisure visit behaviour compared to the influence of childhood socialization: a structural model of relationships.

Those involved with the management of the countryside have an imperative to understand the drivers of behaviour towards it. This is particularly so, since the UK population is largely urban-based and yet still retains an attachment to green open spaces and engagement with the pastoral scene (DEFRA, 2009; Natural England, 2016). The media has been recognised as playing an important role in sustaining this attachment but its relative influence compared to the role of the family, other social groups and education is less well understood in this context. The aim of this research is to provide a measure of the influences that underpin this attachment, specifically to develop a better understanding of the role of mass media as a component of the socializing factors which influence attitudes towards leisure behaviour in the countryside. The measurement and exploration of these influences is based upon a pilot study, followed by a survey of 2775 respondents, in six urban centres in England during 2011 and 2012. The data was analysed in order to investigate the relative role of developmental and mass media influences on countryside leisure behaviour. The cognitive and emotional processes that catalyse these relationships were also evaluated. A structural model of relationships was then developed, which provided predictive measures of the formative influences upon countryside leisure behaviour. Three key findings emerged from the research. The first confirmed that interest in countryside leisure may be derived from early socialization influences but significantly there are sub-groups for whom this early experience is irrelevant. These sub-groups developed their interest in countryside in later adulthood, inspired by the cultural discourse of rural themes represented in the media. Secondly the research identified that the relative influence of early exposure to countryside interests from family and friends is weaker than the direct effect of media on current countryside visit behaviour. Thirdly the predictive relationship suggests that countryside knowledge, the normative and control influences of others and the media, work largely through emotional rather than cognitive processes in their effect upon countryside visit behaviour. A further outcome of the research identified a control influence upon attitudes and engagement with the countryside, driven by pragmatic considerations of countryside as a resource for housing and infrastructure needs. The significant findings from this research make a contribution to knowledge regarding the processes that influence countryside leisure attitudes and behaviour. Specifically, it confirms the importance of developing media strategy that reflects the emotional bond that people have with the countryside and targeting robust market segments, differentiated by media responsiveness and developmental influences. An effective media strategy is particularly important for those sections of the population, who have had little encouragement to engage with the countryside during childhood but are, in adulthood, responsive to its portrayal in the media

Targeting the Side-Chain Convergence of Hydrophobic α‑Helical Hot Spots To Design Small-Molecule Mimetics: Key Binding Features for <i>i</i>, <i>i</i> + 3, and <i>i</i> + 7

The conformational convergence of hydrophobic α-helical hot spots was revealed by analyzing α-helix-mediated protein–protein interaction (PPI) complex structures. The pharmacophore models were derived for hydrophobic α-helical hot spots at positions i, i + 3, and i + 7. These provide the foundation for designing generalizable scaffolds that can directly mimic the binding mode of the side chains of α-helical hot spots, offering a new class of small-molecule α-helix mimetics. For the first time, the protocol was developed to identify the PPI targets that have similar binding pockets, allowing evaluation of inhibitor selectivities between α-helix-mediated PPIs. The mimicry efficiency of the previously designed scaffold 1 was disclosed. The close positioning of this small molecule to the additional α-helical hot spots suggests that the decoration of this series of generalizable scaffolds can conveniently reach the binding pockets of additional α-helical hot spots to produce potent small-molecule inhibitors for α-helix-mediated PPIs

Characterization of Hydrophilic α‑Helical Hot Spots on the Protein–Protein Interaction Interfaces for the Design of α‑Helix Mimetics

The cooperativity index, Kc, was developed to examine the binding synergy between hot spots of the ligand–protein. For the first time, the convergence of the side-chain spatial arrangements of hydrophilic α-helical hot spots Thr, Tyr, Asp, Asn, Ser, Cys, and His in protein–protein interaction (PPI) complex structures was disclosed and quantified by developing novel clustering models. In-depth analyses revealed the driving force for the protein–protein binding conformation convergence of hydrophilic α-helical hot spots. This observation allows deriving pharmacophore models to design new mimetics for hydrophilic α-helical hot spots. A computational protocol was developed to search amino acid analogues and small-molecule mimetics for each hydrophilic α-helical hot spot. As a pilot study, diverse building blocks of commercially available nonstandard L-type α-amino acids and the phenyl ring-containing small-molecule fragments were obtained, which serve as a fragment collection to mimic hydrophilic α-helical hot spots for the improvement of binding affinity, selectivity, physicochemical properties, and synthesis accessibility of α-helix mimetics

Characterization of Hydrophilic α‑Helical Hot Spots on the Protein–Protein Interaction Interfaces for the Design of α‑Helix Mimetics

The cooperativity index, Kc, was developed to examine the binding synergy between hot spots of the ligand–protein. For the first time, the convergence of the side-chain spatial arrangements of hydrophilic α-helical hot spots Thr, Tyr, Asp, Asn, Ser, Cys, and His in protein–protein interaction (PPI) complex structures was disclosed and quantified by developing novel clustering models. In-depth analyses revealed the driving force for the protein–protein binding conformation convergence of hydrophilic α-helical hot spots. This observation allows deriving pharmacophore models to design new mimetics for hydrophilic α-helical hot spots. A computational protocol was developed to search amino acid analogues and small-molecule mimetics for each hydrophilic α-helical hot spot. As a pilot study, diverse building blocks of commercially available nonstandard L-type α-amino acids and the phenyl ring-containing small-molecule fragments were obtained, which serve as a fragment collection to mimic hydrophilic α-helical hot spots for the improvement of binding affinity, selectivity, physicochemical properties, and synthesis accessibility of α-helix mimetics

Targeting the Side-Chain Convergence of Hydrophobic α‑Helical Hot Spots To Design Small-Molecule Mimetics: Key Binding Features for <i>i</i>, <i>i</i> + 3, and <i>i</i> + 7

The conformational convergence of hydrophobic α-helical hot spots was revealed by analyzing α-helix-mediated protein–protein interaction (PPI) complex structures. The pharmacophore models were derived for hydrophobic α-helical hot spots at positions i, i + 3, and i + 7. These provide the foundation for designing generalizable scaffolds that can directly mimic the binding mode of the side chains of α-helical hot spots, offering a new class of small-molecule α-helix mimetics. For the first time, the protocol was developed to identify the PPI targets that have similar binding pockets, allowing evaluation of inhibitor selectivities between α-helix-mediated PPIs. The mimicry efficiency of the previously designed scaffold 1 was disclosed. The close positioning of this small molecule to the additional α-helical hot spots suggests that the decoration of this series of generalizable scaffolds can conveniently reach the binding pockets of additional α-helical hot spots to produce potent small-molecule inhibitors for α-helix-mediated PPIs

Characterization of Hydrophilic α‑Helical Hot Spots on the Protein–Protein Interaction Interfaces for the Design of α‑Helix Mimetics

The cooperativity index, Kc, was developed to examine the binding synergy between hot spots of the ligand–protein. For the first time, the convergence of the side-chain spatial arrangements of hydrophilic α-helical hot spots Thr, Tyr, Asp, Asn, Ser, Cys, and His in protein–protein interaction (PPI) complex structures was disclosed and quantified by developing novel clustering models. In-depth analyses revealed the driving force for the protein–protein binding conformation convergence of hydrophilic α-helical hot spots. This observation allows deriving pharmacophore models to design new mimetics for hydrophilic α-helical hot spots. A computational protocol was developed to search amino acid analogues and small-molecule mimetics for each hydrophilic α-helical hot spot. As a pilot study, diverse building blocks of commercially available nonstandard L-type α-amino acids and the phenyl ring-containing small-molecule fragments were obtained, which serve as a fragment collection to mimic hydrophilic α-helical hot spots for the improvement of binding affinity, selectivity, physicochemical properties, and synthesis accessibility of α-helix mimetics

Characterization of Hydrophilic α‑Helical Hot Spots on the Protein–Protein Interaction Interfaces for the Design of α‑Helix Mimetics

The cooperativity index, Kc, was developed to examine the binding synergy between hot spots of the ligand–protein. For the first time, the convergence of the side-chain spatial arrangements of hydrophilic α-helical hot spots Thr, Tyr, Asp, Asn, Ser, Cys, and His in protein–protein interaction (PPI) complex structures was disclosed and quantified by developing novel clustering models. In-depth analyses revealed the driving force for the protein–protein binding conformation convergence of hydrophilic α-helical hot spots. This observation allows deriving pharmacophore models to design new mimetics for hydrophilic α-helical hot spots. A computational protocol was developed to search amino acid analogues and small-molecule mimetics for each hydrophilic α-helical hot spot. As a pilot study, diverse building blocks of commercially available nonstandard L-type α-amino acids and the phenyl ring-containing small-molecule fragments were obtained, which serve as a fragment collection to mimic hydrophilic α-helical hot spots for the improvement of binding affinity, selectivity, physicochemical properties, and synthesis accessibility of α-helix mimetics

Copper-Mediated Transformation of Organosilanes to Nitriles with DMF and Ammonium Iodide

Cyanation of aryl-, diaryldimethyl-, and styrylsilanes was developed for the first time under copper-mediated oxidative conditions using ammonium iodide and DMF as the combined source of nitrogen and carbon atom of the introduced cyano unit, respectively. The reaction was observed to proceed in a two-step process: initial conversion of organosilanes to their iodo intermediates and then cyanation. This method has a broad substrate scope with high functional group tolerance

Characterization of Hydrophilic α‑Helical Hot Spots on the Protein–Protein Interaction Interfaces for the Design of α‑Helix Mimetics

The cooperativity index, Kc, was developed to examine the binding synergy between hot spots of the ligand–protein. For the first time, the convergence of the side-chain spatial arrangements of hydrophilic α-helical hot spots Thr, Tyr, Asp, Asn, Ser, Cys, and His in protein–protein interaction (PPI) complex structures was disclosed and quantified by developing novel clustering models. In-depth analyses revealed the driving force for the protein–protein binding conformation convergence of hydrophilic α-helical hot spots. This observation allows deriving pharmacophore models to design new mimetics for hydrophilic α-helical hot spots. A computational protocol was developed to search amino acid analogues and small-molecule mimetics for each hydrophilic α-helical hot spot. As a pilot study, diverse building blocks of commercially available nonstandard L-type α-amino acids and the phenyl ring-containing small-molecule fragments were obtained, which serve as a fragment collection to mimic hydrophilic α-helical hot spots for the improvement of binding affinity, selectivity, physicochemical properties, and synthesis accessibility of α-helix mimetics