2026 (Current Year) Faculty Courses School of Life Science and Technology Department of Life Science and Technology Graduate major in Life Science and Technology
Biomolecular Analysis
- Academic unit or major
- Graduate major in Life Science and Technology
- Instructor(s)
- Ryuji Igarashi / Yoshitaka Ishii / Kayo Nozawa / Takakazu Seki
- Class Format
- Lecture (Livestream)
- Media-enhanced courses
- -
- Day of week/Period
(Classrooms) - 3-4 Mon / 3-4 Thu
- Class
- -
- Course Code
- LST.A501
- Number of credits
- 200
- Course offered
- 2026
- Offered quarter
- 1Q
- Syllabus updated
- Apr 6, 2026
- Language
- English
Syllabus
Course overview and goals
An overview will be provided of the theory and applications of NMR spectroscopy, as well as measurement methods and examples of applications to biomolecules (Ishii). An overview will be given of the fundamentals and applications of various magnetic resonance methods for biomolecular and biological measurements (Igarashi). An overview of the fundamentals of biomolecular measurements using mass spectrometry will be provided, including practical measurement methods, particularly for proteomics (Niwa). The basics of vibrational spectroscopy and the optical responses of matter will be described, and advanced interface-specific vibrational spectroscopy and its applications to the structural analysis of interfacial biomolecular systems will be discussed. (Seki). Important insights into macromolecules such as drug–protein complexes and viruses have been obtained by analyzing X-ray diffraction and electron projection images. An overview of the principles and applications of these techniques will be presented (Nozawa).
Course description and aims
By the end of this course, students will be able to:
(1)understand the classical theory of NMR spectroscopy, including the behavior of nuclear spin magnetization based on the Bloch equations, one-dimensional NMR, applications of multidimensional NMR to biomolecules, and an outline of the quantum-theoretical basis of NMR spectroscopy (Ishii).
(2) deepen their understanding of methods and applications for intracellular molecular measurements using NMR, ESR, and ODMR (Igarashi).
(3) understand how to select a mass spectrometer suited to a given objective, and what can and cannot be measured with current proteomics instrumentation, together with its advantages and limitations (Niwa).
(4) understand molecular structure analysis using fundamental spectroscopic methods such as infrared and Raman spectroscopy, as well as interface-specific nonlinear vibrational spectroscopy (Seki).
(5) understand the measurement methods of X-ray crystallography and cryo-electron microscopy, and deepen their understanding of techniques for analyzing the three-dimensional structures of biomolecules and their modes of interaction (Nozawa).
Keywords
NMR, MRI, mass spectrometry, vibrational spectroscopy, quantum sensing, micro- and nanotechnology, molecular imaging, X-ray crystallography, cryo-electron microscopy
Competencies
- Specialist skills
- Intercultural skills
- Communication skills
- Critical thinking skills
- Practical and/or problem-solving skills
Class flow
The class starts with reviews of previous class. Towards the end of class, students are often given exercise problems related to the lecture given that day to solve. To prepare for the class, students should read the course schedule section and check what topics will be covered. Required learning should be completed outside the classroom for preparation and review purposes.
Classes will be basically done in English, but if necessary we will provide supplementary explanation in Japanese.
Classes will be held online using Zoom.
Course schedule/Objectives
| Course schedule | Objectives | |
|---|---|---|
| Class 1 | NMR spectroscopy: (1) Introduction to NMR spectroscopy |
Understanding of basic theory and applications of NMR spectroscopy |
| Class 2 | NMR spectroscopy: (2) Classical theory and 1D NMR |
Understanding of classical theory of NMR spectroscopy and 1D NMR |
| Class 3 | NMR spectroscopy: (3) 2-3D NMR and applications to small molecules, proteins, and imaging |
Understanding of 2-3D NMR and advanced |
| Class 4 | In-cell biomolecular measurements using NMR |
Understanding of the fundamentals and applications of in-cell NMR |
| Class 5 | Mass spectrometry for biomolecules (1) : Fundamentals of mass spectrometry and types of mass spectrometers for biomolecules |
|
| Class 6 | Mass spectrometry for biomecules (2) : Application to proteomics |
Understanding the principles and applications of proteomics analysis |
| Class 7 | Vibrational spectroscopy: (1) Infrared spectroscopy and Raman spectroscopy |
Understanding of basic vibrational spectroscopy and optical responses of materials |
| Class 8 | Vibrational spectroscopy: (2) Introduction to non-linear spectroscopy |
Understanding of non-linear optical responses of materials and interface-specific vibrational spectroscopy |
| Class 9 | Vibrational spectroscopy: (3) Applications to bio-molecular systems |
Understanding of the advanced spectroscopic technique for bio-molecular systems |
| Class 10 | Biomolecular measurements using ESR spectroscopy |
Understanding of the fundamentals and applications of biomolecular measurements by ESR |
| Class 11 | Quantum sensors and ODMR: (1) Introduction and basic understanding |
Understanding of the fundamentals of quantum sensors |
| Class 12 | Quantum sensors and ODMR: (2) Applications to biomolecular measurements |
Understanding of applications of biomolecular measurements by quantum sensors |
| Class 13 | X-ray crystallography and cryo-electron microscopy: (1) Introduction and basic theory |
Understanding of the principle of diffraction and imaging |
| Class 14 | X-ray crystallography and cryo-electron microscopy: (2) Application to biomolecules |
Understanding of applications to macromolecules and their impact |
Study advice (preparation and review)
To enhance effective learning, students are encouraged to spend approximately 100 minutes preparing for class and another 100 minutes reviewing class content afterwards (including assignments) for each class.
They should do so by referring to textbooks and other course material.
Textbook(s)
No textbook is set.
Reference books, course materials, etc.
Handouts will be distributed at the beginning of class when necessary and elaborated on using PowerPoint slides.
Evaluation methods and criteria
Students' knowledge of basic matters, understanding on essential significance and abilities to apply them to problems will be assessed. No midterm and final exams.
Related courses
- LST.A409 ： Physical Biology of the Cell
Prerequisites
Students must have successfully completed Physical Chemistry I, II, and III (number) or have equivalent knowledge.