Course Syllabus and Lesson Plan
SCBM 281
Medical Biochemistry: From Molecules to Cells
(Chemical processes in living system)
Academic Year 2017: 21 August 2017 – 27 November 2017
Course Title: Medical Biochemistry, From Molecules to Cells
Course Code: SCBM 281
Total Credit: 3(3-0-6)
Pre-Requisite:
Duration: First semester
Course Homepage:
http://www.sc.mahidol.ac.th/scbc/webboard/index.php
Course Description:
Structures and functions of biomolecules, protein folding, protein functions, bio-catalysis, enzyme kinetics, citric acid cycle, electron transport and oxidative phosphorylation, anabolism and catabolism of biomolecules in normal and some important pathological stages, regulation of metabolic pathways, flow of genetic information, gene regulation, and molecular techniques with medical applications.
Course Objectives:
At the end of this course, the students will be able to
1. explain chemical processes occurred in living system, structure and functional relationship of biomolecules
2. point out the regulation of metabolic pathways governing the life of a cell
3. know and understand energy metabolism, biosynthesis and degradation in both normal and some important pathological stages
4. emphasize fundamental of genome organization, flow of genetic information and gene regulation
5. learn the principle of molecular techniques relevant to medical applications.
Course Outlines:
See schedule on page
Teaching Methods
Lecture
Teaching Media
• Text book Lehninger, Principle of Biochemistry, 4th or 5th edition,
• CAI, VDO, PowerPoint and/or transparency presentation, can be self-study via web site: http://www.sc.mahidol.ac.th/scbc/webboard/index.php
Evaluation of Student Achievement
Grading system from midterm and final examination
• Midterm written examination (MCQ) 30%
• Final written examination (MCQ) 70%
Total 100%
Students who get a total grade more than 50% are considered successful for this course.
Course Evaluation
Questionnaire about contents, teaching processes, examinations and instructor performance.
Required Textbook
• Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 4th or 5th edition, Worth, New York
Other References
1. Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990.
2. John, W. Baynes and Marek H. Dominiczak, Medical Biochemistry, 2nd edition, Elsevier Mosby, 2005
3. Other equivalent biochemistry textbooks.
Instructors
Lecturer from Department of Biochemistry, Pharmacology, Physiology and Clinician and guest lecturers from outside Faculty of Science
Course Coordinators
Asist. Prof. Dr. Jamorn Somana
Department of Biochemistry, Faculty of Science, Mahidol University
Tel: 0-2201-5601 and 0-2201-5468
Course Syllabus and Lesson Plan
SCBM 282
Medical Biochemistry Laboratory: From Molecules to Cells
(Chemical processes in living system)
Academic Year 2017: 29 August 2017 – 14 November 2017
Course Title: Medical Biochemistry Laboratory
Course Code: SCBM 282
Total Credit: 1(0-3-1)
Pre-Requisite:
Duration: First semester
Course Homepage:
http://www.sc.mahidol.ac.th/scbc/webboard/index.php
Course Description:
Determination of LDH enzyme activity by spectrophotometric method, Determination of liver enzyme activities, DNA isolation and PCR amplification followed with analysis of DNA by gel electrophoresis technique, structures and functions of biomolecules, protein folding, protein functions, bio-catalysis, enzyme kinetics, TCA cycle, electron transport and oxidative phosphorylation, anabolism and catabolism of biomolecules in normal and pathological stages, regulation of metabolic pathways, flow of genetic information, gene regulation, and molecular techniques with medical applications. Starvation
Course Objectives:
At the end of this course, the students will be able to
1. have a laboratories skill on basic techniques in structure and functional relationship of biomolecules
2. gain the knowledge and understand the way to analysis the experimental data
3. work together or have group activities relevant to chemical processes occurred in living system and medical applications
4. acquire necessary knowledge through current available resources and analyze critical problems and data obtained.
Course Outlines:
See schedule on page
Teaching Methods:
Laboratory, Group study, Discussion and assignment
1. Laboratories: Compulsory
There are 4 laboratory exercises designed to broaden the students’ skill and knowledge. These are 1) determination of LDH enzyme activity and studying LDH enzyme kinetics by spectrophotometric method 2) determination of liver enzyme activities 3) Determination of cholesterol and triglyceride in serum lipoproteins 4) DNA isolation, PCR amplification and analysis of DNA by gel electrophoresis technique.
2. Small Group or Conferences: Compulsory
There are 3 small group discussions. The sessions involve discussion on problem sets related to the topics SCID 141 and some clinical cases. Student presentation and discussion will be focused and all sessions will have either pre- or post discussion quizzes.
3. Problem-Based Learning: Compulsory
Problem-based scenario will be given to initiate group activities in the discussion and self-study sessions to find out a possible explanation for the problem. Developments of conceptual thinking skill and integration of information are the main objective.
4. Tutorials: Not Compulsory
There are 3 tutorial periods to cover the basic concepts of the course. Tutorial period is provided to help students better understand the topics and/or clarify some points after their self- or group-study. Therefore, students are expected to go through the topics and prepare questions prior to each tutorial discussion. Questions for each tutorial session can be posted at the web-board (see course homepage) or can be submitted directly to the lecturer(s). All tutorials will be held at lecture hall.
5. CAI (CD and VDO): Compulsory
There are 1 CAI media available in this course, i.e. structure folding and build block, high throughput automated system, and molecular diagnosis, PCR and sequencing technique. These learning materials will be installed in the computer system and the students can access and study during free time. One CAI-media on PCR and DNA sequencing techniques is used in a class discussion.
Teaching Media:
• Laboratory manual of the course
• Text book Lehninger, Principle of Biochemistry, 4th or 5th edition,
• CAI, VDO, PowerPoint and transparency presentations, can be self study via web site: http://www.sc.mahidol.ac.th/scbc/webboard/index.php
Evaluation of student achievement:
Grading system from written examination and work assignments or performance in the activities
Process 80%
Small group (5% x3) 15%
PBL (10% x 2) 20%
Laboratories (10% x 4) 40%
CAI (5%) 5%
Knowledge 20%
From written examination (Midterm 10% and Final 10%)
Out of the total 100%, students who get a grade more than 60% are considered successful for this course
Course Evaluation:
Questionnaire about contents, teaching processes, examinations and Instructor performance.
Required Textbook
• Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 4th or 5th edition, Worth, New York
Other References:
1. Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990.
2. John, W. Baynes and Marek H. Dominiczak, Medical Biochemistry, 2nd edition, Elsevier Mosby, 2005
3. Other equivalent biochemistry textbooks.
Instructors:
Lecturer from Department of Biochemistry
Course Coordinators:
Assist. Prof. Dr. Jamorn Somana
Department of Biochemistry, Faculty of Science, Mahidol University
Tel: 0-2201-5601 and 0-2201-5468
SCBM 281, 282 Schedule for the First Semester, Year 2017, Student Group SCBM
Day / Date / Time / Activity / Room / Instructor /Monday / 21 Aug 17 / 8.30-10.30 / Course Orientation
Lecture 1: DNA Replication and Repair / SC1-161 / Jamorn(BC), Laran(BC) /
10.30-12.30 / Lecture 2: RNA and Protein Synthesis / SC1-161 / Laran (BC) /
Tuesday / 22 Aug 17 / 13.30-15.30 / Lecture 3: Gene Expression and Regulation / SC1-161 / Laran (BC) /
15.30-17.30 / Lecture 4: DNA Technology / SC1-161 / Laran (BC) /
Monday / 28 Aug 17 / 8.30-10.30 / Lecture 5: Structure and Functions of Biomolecules / SC1-161 / Kittisak (BC) /
10.30-12.30 / Lecture 6: Protein Structure and Concept of Folding / SC1-161 / Kittisak (BC) /
Tuesday / 29 Aug 17 / 13.30-15.30 / CAI: Molecular Diagnostic, PCR and DNA Sequencing / SC1-161 / Laran (BC) & TA /
Monday / 4 Sep 17 / 8.30-10.30 / Lecture 7 Biocatalysis and Enzyme Kinetics / SC1-161 / Kittisak (BC) /
10.30-12.30 / Lecture 8: Protein Structure and Function / Molecular Assembly / SC1-161 / Kittisak (BC) /
Tuesday / 5 Sep 17 / 13.30-14.30 / Lab 1: DNA Isolation, PCR, Electrophoresis – Brief Lab / SC3 Lab / Laran (BC) and TA /
14.30-16.30 / Lab 1: DNA Isolation, PCR, Electrophoresis – Experiment / SC3 Lab /
Monday / 11 Sep 17 / 9.30-11.30 / Lecture 9: Carbohydrate Metabolism / SC1-161 / Wilai(BC) /
MU congregation day 12 September 2017 /
Monday / 18 Sep 17 / 9.30-11.30 / Conference 1: Active Learning Lesson: Molecular Technology in Medicine / SC1-161 / Laran (BC) & TA /
Tuesday / 19 Sep 17 / 13.30-14.30 / Lab 2: Enzyme LDH – Brief Lab / SC3 Lab / Kittisak (BC) & TA /
14.30-16.30 / Lab 2: Enzyme LDH – Experiment /
Monday / 25 Sep 17 / 9.30-11.30 / Lecture 10: Citric Acid Cycle / Oxidative Phosphorylation / SC1-161 / Tuangporn(BC) /
Tuesday / 26 Sep 17 / 13.30-15.30 / Conference 2: Hemoglobin Structure and Function / SC1-161 / Kittisak (BC) & TA /
Monday / 2 Oct 17 / 8.30-10.30 / Lecture 11: Amino Acids Metabolism / SC1-161 / Wilai(BC) /
10.30-12.30 / Lecture 12: Nutrition / SC1-161 / Wilai(BC) /
Tuesday / 3 Oct 17 / 13.30-15.30 / PBL 1: Hunger Strike / SC1-161+ / Jamorn(BC), Tuangporn(BC) and TA /
Monday / 9 Oct 17 / 9.30-11.30 / Lecture 13: Nucleotide metabolism / SC1-161 / Tuangporn(BC) /
Tuesday / 10 Oct 17 / 13.30-15.30 / Tutorial 1: Q&A Structure & Function, Gene regulation & DNA technology / SC1-161 / Kittisak(BC), Laran(BC), /
Midterm Examination 16-20 October 2017 /
Day / Date / Time / Activity / Room / Instructor /
Chulalongkorn Memorial Day 23 October 2017 /
Tuesday / 24 Oct 17 / 13.30-15.30 / Conference 3: Active Learning Lesson: Diabetes / SC1-161 / Jamorn(BC) and TA /
Monday / 30 Oct 17 / 8.30-10.30 / Lecture 14: Lipid Metabolism / SC1-161 / Jamorn(BC) /
10.30-12.30 / Lecture 15: Heme and Minerals Metabolism / SC1-161 / Jamorn(BC) /
Tuesday / 31 Oct 17 / 13.30-14.30 / Lab 3: Determination of Serum Lipids – Brief Lab / SC3 Lab / Jamorn(BC) and TA /
14.30-16.30 / Lab 3: Determination of Serum Lipids – Experiment / SC3 Lab /
Monday / 6 Nov 17 / 9.30-11.30 / Lecture 16: Integration and Regulation of Metabolism / SC1-161 / Jamorn(BC) /
Tuesday / 7 Nov 17 / 13.30-15.30 / PBL 2: Hunger Strike / SC1-161+ / Jamorn(BC), Tuangporn(BC) and TA /
Monday / 13 Nov 17 / 9.30-11.30 / Lecture 17: Biochemistry Knowledge and Medicine / SC1-161 / Jamorn(BC) /
Tuesday / 14 Nov 17 / 13.30-14.30 / Lab 4: Determination of Liver Enzyme Activities – Brief Lab / SC3 Lab / Tuangporn(BC) and TA /
14.30-16.30 / Lab 4: Determination of Liver Enzyme Activities – Experiment / SC3 Lab /
Monday / 27 Nov 17 / 9.30-11.30 / Tutorial 2: Q&A Metabolism, Medical Application / SC1-161 / Wilai(BC), Tuangporn(BC), Jamorn(BC) /
Final Examination 12-22 December 2017 /
LESSON PLAN
Lecture 1: DNA replication and repair
Instructor: Laran T. Jensen, Biochemistry, Faculty of Science
Date/Time: Monday, 21 August 2017, 8.30-10.30
Room: SC1-161
Learning Objectives:
Students should be able to
1. list factors required for DNA replication
2. explain the functions of enzymes and protein in DNA replication
3. define the meanings of leading and lagging strand DNA synthesis, and okazaki fragment
4. explain the concepts of mutation and repair mechanism
Content Outlines:
1. Flow of genetic material, the central dogma
2. DNA replication, semi-conservative replication, origin of replication
3. replication fork Leading and lagging strand synthesis, okazaki fragment
4. Functions of proteins and enzymes required for DNA replication
5. Mutation and repair mechanism
Leading questions:
- What is the semi-conservative DNA replication?
- How can replication of mammalian DNA which is much bigger than the prokaryotic DNA being carried out in just a few minutes?
- What are the functions of topoisomerase, helicase, single stranded binding protein, primase, DNA polymerase and DNA ligase?
- What are the functions of DNA polymerase I and III?
- Why DNA replication is so accurate?
Learning Organization:
1. Lecture 110 min.
2. Q&A 10 min.
3. Study from the course textbook
Learning Materials provided:
• List of suggested readings.
Student Assessment:
Multiple-choice questions with short (written) explanations.
LESSON PLAN
Lecture 2: RNA and protein synthesis
Instructor: Laran T. Jensen, Biochemistry, Faculty of Science
Date/Time: Monday, 21 August 2017, 10.30-12.30
Room: SC1-161
Learning objectives:
Students should be able to
RNA metabolism
1. list components required for transcription
2. explain the component and function of RNA polymerase
3. explain the function of promoter
4. describe steps of transcription
5. describe posttranscriptional modification of RNAs
Protein synthesis
1. explain the terms “codon”, anticodon”, wobble base and meaning of genetic code
2. discuss the factors require for translation
3. explain steps of translation
4. explain how the peptide bonds are form between amino acids during translation
5. explain the actions of some antibiotics on protein synthesis
6. discuss how nuclear encoded proteins are transported to organelles
Content Outlines:
RNA metabolism
1. Transcription (initiation, elongation and termination)
2. functions of various proteins and enzymes required for transcription
3. Promoter recognition and RNA polymerase
4. RNA processing:mRNA, rRNA and tRNA
5. Reverse transcriptase
Leading questions:
- What determine the boundary of gene?
- What is the function of TATA-box?
- What are the functions of sigma factor and core RNA polymerase?
- What is the importance of 5’-capping, intron removal and 3’-polyadenylation?
- Why can some single-copied genes produce multiple isoforms of encoded proteins?
Protein synthesis
1 Genetic code, triplet codon, open reading frame
2. Ribosome structure and component
3. tRNA
4. Translation initiation, elongation and termination
5. Effect of antibiotics on protein synthesis
6. Protein targeting
Leading questions:
- What is the meaning of non-overlapping triplet codon?
- How is mRNA stabilized on the ribosome?
- What is a maximum number of genetic codes that are recognized by tRNA?