Biochemistry

This course covers amino acids, the fundamentals of protein structure, isolation and purification of proteins, modification of proteins, and methods of determining protein conformation. It also covers the basics of enzyme catalysis and kinetics with specific case studies. Other topics include ion transport, and other transport proteins, and the utilization of proteins and soluble cofactors to generate and store metabolic energy. Students learn the basics of metabolism in glycolysis and the citric acid cycle, as well as ATP synthesis and membrane bound electron transfer in mitochondria. Chloroplasts in plants and algae, and molecular motors, such as muscles, that consume metabolic energy are also covered. 

This course covers the different types of membrane proteins, how they can be overexpressed and purified from a host cell, and how different methods can be used to analyze their structure and function. The course includes predictions and practical investigations of protein folding in a membrane, as well as a shorter project where you under guidance plan and carry out cloning and overexpression of a membrane protein of your choice.  Course lectures address the three different main types of membrane proteins and associated cellular processes: transport and transporters, signal transduction and receptors, bioenergetics, and photosynthetic and respiratory proteins. Lectures dealing with methods for theoretical modeling of membrane protein structure, fusion protein techniques, X-ray crystallography, heterologous expression, solubilization, and purification of membrane proteins are also included in the course. Laboratory sessions, exercises, and project work are used to determine the transmembrane topology of a protein starting with a model of the protein based on sequence information and theoretical methods. This is followed by experimental determination using genetic construction and expression of a fusion protein of the membrane protein and a marker protein in a bacterial system which is subsequently analyzed.  An individually planned and executed project on protein expression provides practice in literature searching, project planning, and documentation. The project is to be concluded with a poster presentation.

To give students the opportunity to understand the key aspects of chemistry that are relevant to biochemistry, including the important structural implications of biologically relevant macromolecules, thermodynamics, and chemical reactions together with their reaction kinetics.

This course addresses how modern techniques of structural and chemical biology are being used to solve biological problems. It draws on multiple aspects of macromolecular biochemistry including nucleic acid structure and interactions, signaling proteins, and membrane proteins.  The course demonstrates how this knowledge can be used in drug discovery and protein design in biotechnology. Topics include mechanisms of reversible and irreversible enzyme inhibitors, ligand binding, protein folding, the molecular basis for protein function, regulation of protein activity, cell signaling, and proteomics. Assessment: Tests count 40%; practicals, tutorials essays, and assignments count 10%; one 3-hour examination written in June counts 50%. A subminimum of 40% in the examination is required.

This course provides a firm and rigorous foundation in current concepts of the structure and functions of biomolecules in molecular cellular biology. These fundamental concepts form the basis of almost all recent advances in biological and biomedical sciences. The course introduces and discusses biomolecular structures and functions (including protein, carbohydrates, lipid, and nucleotides) and how these biomolecules play roles in biological processes including cellular biocatalyst and metabolism. Practical sessions provide experience in data interpretation and learning of basic laboratory techniques.

This course describe the structures of biological macromolecules, particularly proteins, in relation to their functions in catalysis, ligand binding, membrane transport, and ability to form and function as complexes, and to illustrate the types of experimental techniques used to study macromolecular structure and function. It develops personal skills appropriate to a third-year biological science student, including competence in a range of laboratory techniques; the ability to analyze scientific papers; familiarity with the use of libraries and databases; the ability to present the results of experimental work concisely and accurately, both numerically and in writing, and to write about biochemical and molecular biological topics in a clear and well-organized manner.

This course provides individual research training for students in the Junior Year Engineering Program through the experience of belonging to a specific laboratory at Tohoku University. Students are assigned to a laboratory with the consent of the faculty member in charge. They participate in various group activities, including seminars, for the purposes of training in research methods and developing teamwork skills. The specific topic studied depends on the instructor in charge of the laboratory to which each student is assigned. The methods of assessment vary with the student's project and laboratory instructor. Students submit an abstract concerning the results of their individual research each semester and present the results near the end of this program.

This course provides an introduction to ocean properties and processes. Topics include processes that exchange energy and water within the Earth system; main sources, sinks, and pathways of material; temperature, salinity, and density structure; temperature-salinity diagram; waves and tide generation; Eulerian and Lagrangian co-ordinate systems; hydrothermal circulation; biogeochemical cycling of oxygen, carbon dioxide and nutrients; biogenic sediments; volume transport and fluxes of material; and instrumentation used in oceanography.

The Individual Research Training Senior (IRT Senior) Course is an advanced course of the Individual Research Training A (IRT A) course in the Tohoku University Junior Year Program in English (JYPE) in the fall semester. Though short-term international exchange students are not degree candidates at Tohoku University, a similar experience is offered by special arrangement. Students are required to submit: an abstract concerning the results of their IRT Senior project, a paper (A4, 20-30 pages) on their research at the end of the exchange term, and an oral presentation on the results of their IRT Senior project near the end of the term.

The course covers in depth the chemistry of three major classes of biologically important molecules; carbohydrates, peptides and proteins, and nucleic acids. In addition, the course provides an introduction to molecular imaging and covers methods for labelling of biomolecules with fluorescent dyes and radionuclides.