Ÿ Biomolecular Science Course

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Classes in this list are given in English.

Class Name

Credit

Lecturer(s)

Semester

Remars

Advanced Biophysical Chemistry

2-0-0

Tanaka, et al,

Autumn

O

Advanced Biochemistry

2-0-0

Kitamura, et al.

Autumn

O

Advanced Course of Biology

2-0-0

Ohsumi, et al.

Autumn

O

Biotechnology Frontier

2-0-0

Spring

O

Advanced Course of Biological Recognition and Signaling II

2-0-0

Saitoh

Autumn

O

Asymmetric Synthesis

2-0-0

Kobayashi

Autumn

O

Bioscience and Biotechnology International Communication I

2-0-0

 

Spring

O

Advanced Course of Bioscience Communication

2-0-0

Arimura

Autumn

 

Advanced Bioorganic Chemistry

2-0-0

Hashimoto, et al.

Autumn

E

Advanced Molecular Biology

2-0-0

Handa, et al.

Autumn

E

Advanced Bioengineering

2-0-0

Unno, et al.

Autumn

E

Bioscience Frontier

2-0-0

 

Spring

E

Synthesis of Bioactive Substances

2-0-0

Yuasa

Autumn

E

Biomolecular Systems

2-0-0

Ikai

Spring

E

Applied Microbiology

2-0-0

Ishikawa

Spring

E

Structure and Function of Supramolecules

2-0-0

Arisaka

Spring

E

Advanced Cell Biochemistry

2-0-0

Komada

Spring

E

Bioscience and Biotechnology International Communication II

2-0-0

Spring

E

"E" or "O" in the remarks column shows that those classes are open in even or odd year, respectively. The classes without such symbols are open every year.


<2003 Autumn Semester>


Advanced Biophysical chemistry (2-0-0) Odd year

Prof. Nobuo TANAKA, Prof. Yoshimi TSUCHIYA, and Prof. Hiroyuki OHTANI

(Aim)

Therecent development on biophysical chemistry makes it possible to elucidate the relationship between the structure and function of the biological molecule.  The present lecture states about the X-ray diffraction, NMR and light absorption with their application to the biological materials.  We hope that the attendances have understood the basic principle of chemistry, physics and biology.   

(Schedule)

1. Fundamental of X-ray Analysis

      Diffraction of X-ray by crystals and chain molecules

2. Description of Proteinfs structure

      Secondary structure, Tertiary structure, Domain structure

3. Characterization of proteinfs structures(1)

      Prosthetic groups 

4. Characterization of proteinfs structures(2)

     Thermostabilty of the enzymes

5. Fundamentals of NMR (1)

      Time-dependent perturbation, transition probability

6. Fundamentals of NMR (2)

      Nuclear magnetic moment, Zeemann effect and selection rule

7. Experimental principles (1)

      Chemical shift and spin-spin interaction

8. Experimental principles (2)

      Experimental system, relaxation times T1,T2 , pulse NMR

9. Light absorption of visual pigments

      Interactions between light and molecules are discussed by using the concepts of molecular orbital and electronic

transition.

10. Reactions of visual pigments in the excited states

Relaxation processes of chromophore molecules in the excited state are summarized.

11. Sequential reactions in visual cells

The signal amplification in visual cells are discussed in terms of chemical reactions.

12. Time-resolved spectroscopy of living cells

How to measure the in vivo reactions is shown.

Advanced Biochemistry (2-0-0) Odd year

Prof. Naomi KITAMURA, Associate Prof. Yuji SAITOH, and Associate Prof. Fumio ARISAKA

 (Aim)

This course will be given in English. Major areas of contemporary biochemistry will be covered to help understand the chemical basis of life. The themes include (i) macromolecular assembly, (ii) signal transduction, and (iii) posttranslational modification.

 (Schedule)

1. Protein structure and folding

2. Protein motif

3. Protein-protein interactions

4. Macromolecular assembly

5. Growth factors and receptors

6. Cell signaling pathways

7. Intracellular trafficking

8. Cell growth regulation

9. Posttranslational modification and vitamins

10. Protein cross-linking and protein disulfide isomerase

11. Protein cross-linking and transglutaminase

12. Protein-kinases and phosphatases

Advanced Course of Biology (2-0-0) Odd year

Keita OHSUMI, Shiro KOHSHIMA and Kazuhiko OHSHIMA

 (Aim)

This course will feature the variety aspects of biological phenomena. Major areas of contemporary biology will be covered to help understand the modern biology. The themes include (1) Cell Biology, (2) Ecology, and (3) Molecular Evolution. This course will be given in English.

 (Schedule)

1. Cell biology (especially cell-cycle control and cell division)

2. Ecology (especially ecology of snow and ice environments)

3. Molecular Evolution (especially genome evolution and comparative genomics).

Advanced Course of Biological Recognition and Signaling II (2-0-0) Odd year

Assoc. Prof. Yuji SAITO

(Aim)

Students will learn the up-to-date knowledge and the ways to carry out research about biological signal transduction. This object could be attained not only from the lectures given by the instructor but also by actively participating in a series of presentations given by fellow students.

(Schedule)

1. Give basic and general understanding about Biological Signal Transduction. (2 weeks)

Explain various receptors and molecules involved in different biological signal transduction pathways, and cross-talks among them.

2. Discuss about various oncogenes and tumor suppressors with regard to apoptosis, differentiation

and cancer, based on topics published in recent literatures. (2 weeks)

3. Students are expected to make a bit formal presentations about a series of subjects chosen from current literature. Students will

learn from this experience how to write and read papers as well as how to give a talk in conferences. (8 weeks)

(How to grade)

Students are expected to attend lectures as often as possible, and actively participate in the discussion about the topics presented by fellow students.

Asymmetric Synthesis (2-0-0) Odd year

Associate Prof. Yuichi KOBAYASHI

(Aim)

Asymmetric reaction is one of the most powerful methods to prepare chiral compounds.   Presented herein is some of the efficient asymmetric reactions by which high enantiomeric excess of the products is attained.   The principle and the mechanism for the creation of chiral centers in the molecules are also discussed. 

(Schedule)

 1. Fundamental Aspects of Asymmetric Synthesis

 2. Preparation of Chiral Compounds by means of Optical Resolution, Asymmetric Synthesis, Chiral

Pool Method, Reactions using Enzymes

 3. Diastereoselection and Enantioselection

 4. Selectivity in the Enolate Formation and the Asymmetric Alkylation

 5. Asymmetric Aldol Condensations: Part 1

 6. Asymmetric Aldol Condensations: Part 2

 7. Catalytic Asymmetric Reactions: Part 1:

Hydrogenation, Isomerization, Allylic Substitution

 8. Catalytic Asymmetric Reactions: Part 2:

Cyclopropanation, Diels-Alder Reaction

 9. Asymmetric Epoxidation

10. Transformations of Epoxides

11. Asymmetric Dihydroxylation

12. Asymmetric Reactions of Compounds with Symmetry Elements

13. Chiral Pool Method

14. Asymmetric Synthesis of Biologically Active Compounds

15. Summary

 

(How to grade)

Attendance and report


Biomolecular Systems (2-0-0) Even Years

Prof. Atsushi IKAI

(Aim)

Course will be given in English. Physical principle of macromolecular association and experimental methods to study the association process will be reviewed starting from the basics of macromolecular science and intermolecular forces.

 1. Introduction to biological and synthetic molecular systems

 2. Structure formation and expression of functions

 3. Visualization of molecular systems

 4. Fundamentals of intermolecular forces (1)

 5. Fundamentals of intermolecular forces (2)

 6. Protein folding and self assembly (1)

 7. Protein folding and self assembly (2)

 8. Kinetics (1) (Differential equations)

 9. Kinetics (2) (Physical background)

 10. Examples: Fatty acid synthetase etc.

 11. Examples: Nucleosomes etc.

 12. Examples: Cell membrane etc.

 (If time allows the following will be scheduled)

 13. Guest seminar

 14. Guest seminar

 15. Discussion

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