授業「キャンプ実習」に関する研究(3) : 3ヶ年の基礎研究比較と総合評価

This research of the third stage executed mainly the comparison of the basic researches into three years. The chief purpose was clarification of a universal part of three years. The results were summarized as follows : 1. The reason for participation was "Cheap expenditure" and "Course credit". The expected program was "Observation of constellation" and "Outdoors cooking". The expectation in the practice was "Memories-making", "Experience of happiness", "Harmony with nature", "Build healthy human relationships" and "Acquisition of knowledge and technology". Own acquisition target was "Basic technique" and "Safe procedure". 2. A new problem was a discovery of the method of thoroughly improving student\u27s knowledge and technologies. 3. Student\u27s leadership was extent to be able to do "Life guidance" and "Standard program". 4. The factor analysis has extracted the following six factors. "Mutual guidance and Consideration", "Charge program and Satisfaction", "Inspiration and Commitment", "Health condition and Stability", "Appropriate amount of activity" and "Guidance of program and Uneasiness". 5. The attitude to the student\u27s outdoors activities has changed independent and positively. The practice gave the good influence to student\u27s "Standpoint and Attitude". The practice was effective in "Understanding and Goodwill" to nature

Identification of a strong binding site for kinesin on the microtubule using mutant analysis of tubulin

The kinesin-binding site on the microtubule has not been identified because of the technical difficulties involved in the mutant analyses of tubulin. Exploiting the budding yeast expression system, we succeeded in replacing the negatively charged residues in the α-helix 12 of β-tubulin with alanine and analyzed their effect on kinesin–microtubule interaction in vitro. The microtubule gliding assay showed that the affinity of the microtubules for kinesin was significantly reduced in E410A, D417A, and E421A, but not in E412A mutant. The unbinding force measurement revealed that in the former three mutants, the kinesin–microtubule interaction in the adenosine 5′-[β,γ-imido]triphosphate state (AMP-PNP state) became less stable when a load was imposed towards the microtubule minus end. In parallel with this decreased stability, the stall force of kinesin was reduced. Our results implicate residues E410, D417, and E421 as crucial for the kinesin–microtubule interaction in the strong binding state, thereby governing the size of kinesin stall force