Hiroshima University Syllabus

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Academic Year 2024Year School/Graduate School Graduate School of Integrated Sciences for Life (Master's Course) Division of Integrated Sciences for Life Program of Mathematical and Life Sciences
Lecture Code WG123001 Subject Classification Specialized Education
Subject Name 分子生物物理学
Subject Name
Subject Name in
Molecular Biophysics
タテ シンイチ,ヤスダ キョウタ,オオマエ エイジ,カタヤナギ カツオ
Campus Higashi-Hiroshima Semester/Term 1st-Year,  First Semester,  1Term
Days, Periods, and Classrooms (1T) Tues1-2,Fri1-2:Follow the instruction by the class instructor.
Lesson Style Lecture Lesson Style
(More Details)
In this lecture course, we are going to teach you the basic experimental approaches to quantitatively understand the events in life, with emphasis on protein researches. Advancements that emerged over recent years will be delivered to awaken your interest in topical questions. All lectures are presented in English.    
Credits 2.0 Class Hours/Week   Language of Instruction E : English
Course Level 5 : Graduate Basic
Course Area(Area) 26 : Biological and Life Sciences
Course Area(Discipline) 03 : Basic Biology
Eligible Students Master course students
Keywords biophysics; cell; bio-molecules; instrumentation and measurement 
Special Subject for Teacher Education   Special Subject  
Class Status
within Educational
(Applicable only to targeted subjects for undergraduate students)
The course aims to give you the basic ideas how to obtain quantitative insights into how proteins work in vitro and in vivo, which constitute the principal issues in life science. You may also learn how to combine your basic knowledge together to grasp the various aspects of proteins.  
Criterion referenced
(Applicable only to targeted subjects for undergraduate students)
Class Objectives
/Class Outline
Students are expected to gain the basic concepts in the experimental approaches required in biophysics. They will become familiar with the interdisciplinary research flavor through the lectures.  
Class Schedule lesson1: Introduction to protein chemistry: Protein structure-function relationship
lesson2: NMR(1): NMR techniques to solve the solution structure of protein
lesson3: NMR(2): NMR techniques to solve the protein structural dynamics
lesson4: X-ray(1) Crystallography of single crystal

lesson5: X-ray(2) Treatment of Symmetry   
lesson6: X-ray(3) Patterson Function
lesson7: X-ray(4) Anomalous Dispersion
lesson8: Enzymology(1): Thermodynamic analysis of structural stability of enzymes (1)
lesson9: Enzymology(2): Thermodynamic analysis of structural stability of enzymes (2)
lesson10: Enzymology(3): Thermodynamic and kinetic analyses of enzyme functions (1)
lesson11: Enzymology(4):Thermodynamic and kinetic analyses of enzyme functions (2)
lesson12: Cell biology experiments(1)
lesson13: Cell biology experiments(2)
lesson14: Cell biology experiments(3)
lesson15: Cell biology experiments(4)

The students are required to submit the reports on the relating subjects the lectures, at the end of the course.

1-3: Tate, 4-7: Katayanagi, 8-11: Ohmae, 12-15: Yasuda 
PC or AV used in
(More Details) PC projector and handouts in need 
Learning techniques to be incorporated  
Suggestions on
Preparation and
Grasp the essence in the classes. Think deeply in solving the problems given in the final of the lecture course.  
Grading Method The reports on the problems given at the final of the course will be evaluated, besides the engagement in the class discussion.  
Practical Experience  
Summary of Practical Experience and Class Contents based on it  
Message Active discussion in the classes. Questions in a class are recommended. 
Please fill in the class improvement questionnaire which is carried out on all classes.
Instructors will reflect on your feedback and utilize the information for improving their teaching. 
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