BMB533: Molecular biology and protein chemistry
The Study Board for Science
Teaching language: Danish or English depending on the teacher
EKA: N200039112, N200039122, N200039102
Assessment: Second examiner: None, Second examiner: External
Grading: Pass/Fail, 7-point grading scale
Offered in: Odense
Offered in: Autumn
Level: Bachelor
STADS ID (UVA): N200039101
ECTS value: 10
Date of Approval: 06-03-2025
Duration: 1 semester
Version: Archive
Entry requirements
The course cannot be followed by students who have followed BMB504 or if BMB504 are part of the course of study.
Academic preconditions
The course builds on the subject matter covered in the courses BMB544 and BMB531
Students taking the course are expected to:
Course introduction
The aim of the course is to enable the student to gain a basic understanding of molecular biology in all living organisms. We will study the flow of genetic information from DNA to RNA to proteins in prokaryotes and eukaryotes, and the regulation of these processes.
Expected learning outcome
The learning objectives of the course is that the student demonstrates the ability to:
- Know how to use correctly general terminology within the fields of genetics, molecular biology and protein chemistry.
- Explain the Central Dogma of the flow of information from genes to proteins.
- Explain connection between nucleic acid structure and function in the Central Dogma information flow.
- Describe the basic steps in DNA replication and transcription, and mRNA translation to proteins.
- Describe the combinations of enzyme complexes that are involved in DNA replication and transcription, and mRNA translation to proteins.
- Understand the principles of gene regulation.
- Give detailed, specific examples of these processes.
- Distinguish the differences between the molecular processes governing these processes in prokaryotes and eukaryotes.
- Sketch the mechanisms involved in homologous and specific recombination.
- List the main causes of mutation and the consequences of these at the molecular and cellular levels and their potential effects on the whole organism.
- Demonstrate knowledge of general techniques in molecular biology and gene technology.
- Describe the chemical structures of the twenty common amino acids, and how modification of these alters protein structure and function.
- Differentiate between primary, secondary and tertiary structures of proteins and describe quaternary interactions within protein complexes.
- Use the programs VMD for visualizing macromolecular structures, and its application in discovering details of molecular interactions.
- Describe the folding, misfolding and degradation of proteins, and how deviations in these molecular pathways can lead to disease.
- Attain knowledge of modern methodology in protein chemistry, protein purification, characterization and their analysis using bioinformatics.
- Demonstrate knowledge of how proteins interaction with other biological macromolecules during the execution of physiological processes in the cell. This includes an understanding of how proteins function in receptor signalling and in sensory system.
- Independently search and find relevant information to answer questions concerning the topics covered on this course.
Content
The following main topics are contained in the course:
- Protein structure, folding and function
- Protein function in the context of physiology
- Post translational modification of proteins
- Protein degradation
- Methods in protein chemistry
- Genome organization in prokaryotes and eukaryotes
- Information flow from gene to protein
- Structure and function of nucleic acids (DNA og RNA)
- DNA replication, including regulation of DNA synthesis
- Mechanisms of DNA recombination
- Mutations and repair of DNA
- Mechanisms of transposition
- Synthesis of RNA via DNA transcription
- Regulation of gene expression
- RNA processing and mRNA splicing
- Composition of ribosomes and their function in protein synthesis
- Protein localization and export
- Control of the cell cycle by proteins
- Proteins involved in G-protein coupled receptor signaling and Tyrosine kinase receptor signaling
- Antibiotics and cytotoxins
- Fundamental metods used in molecular biology, including PCR, DNA sequencing, gene cloning.
Literature
- Berg, Tymoczko og Stryer: Biochemistry, latest edition.
- Additional material will be selected from year to year.
See itslearning for syllabus lists and additional literature references.
Examination regulations
Prerequisites for participating in the exam a)
Timing
Autumn
Tests
Participation in laboratory exercises
EKA
N200039112
Assessment
Second examiner: None
Grading
Pass/Fail
Identification
Full name and SDU username
Language
Normally, the same as teaching language
Examination aids
To be announced during the course
ECTS value
0
Additional information
The prerequisite examination is a prerequisite for participation in exam element a).
Exam element a)
Timing
Autumn
Prerequisites
| Type | Prerequisite name | Prerequisite course |
|---|---|---|
| Examination part | Prerequisites for participating in the exam a) | N200039101, BMB533: Molecular biology and protein chemistry |
Tests
Written reports for laboratory exercises
EKA
N200039122
Assessment
Second examiner: None
Grading
Pass/Fail
Identification
Full name and SDU username
Language
Normally, the same as teaching language
Examination aids
To be announced during the course
ECTS value
2
Additional information
4-5 are to be handed in during the course.
The re-examination consists of submission of the parts of the report which have not been approved.
The re-examination consists of submission of the parts of the report which have not been approved.
Exam element b)
Timing
January
Tests
Written exam
EKA
N200039102
Assessment
Second examiner: External
Grading
7-point grading scale
Identification
Student Identification Card - Name
Language
Normally, the same as teaching language
Duration
4 hours
Examination aids
All common aids are allowed e.g. books, notes, computer programmes which do not use internet etc.
Internet is not allowed during the exam. However, you may visit the course site in itslearning to open system "DE-Digital Exam". If you wish to use course materials from itslearning, you must download the materials to your computer the day before the exam. During the exam you cannot be sure that all course materials is accessible in itslearning.
ECTS value
8
Indicative number of lessons
Teaching Method
Planned lessons
Total number of planned lessons: 86
Hereof:
Common lessons in classroom/auditorium: 40
Team lessons in classroom 30
Team lessons in laboratory 16
The course consists of lectures, group sessions, and laboratory exercises, all designed to support students' learning in protein chemistry and molecular biology.
The lectures introduce key topics in the chemistry of amino acids and nucleotides, as well as the synthesis of polypeptides and nucleic acids, including their primary, secondary, tertiary, and quaternary structures. These topics are presented through examples of structural changes in nucleic acids and proteins caused by interactions with other biomolecules in various cellular and physiological contexts. Central molecular mechanisms involved in cellular (prokaryotic and eukaryotic) regulation of signal transduction, replication, transcription, and translation are also covered. The lectures supplement the textbook, which students are expected to study independently. Group notes and discussions are recommended as part of the learning strategy.
The team lessons focus on developing practical skills and competencies in protein chemistry and molecular biology. Students work on problem-solving and case studies, which are partially or fully solved before the sessions. During the sessions, students receive feedback on their solutions through discussions with instructors and peers.
The laboratory exercises provide students with practical knowledge of methods and techniques used in the study of nucleic acids and proteins. These exercises are divided into:
a) training in the use of computer software for structural analysis of DNA, RNA, and proteins, and b) laboratory work involving the purification and analysis of DNA.
The exercises require students to come prepared with an understanding of protocols and methods. Data from the exercises are processed in groups and reported individually.
Other planned teaching activities include independent textbook study, problem-solving, and comprehension of laboratory protocols. Students are expected to work independently or in groups to gain a deeper understanding of the course topics. Leading up to the written exam, students are expected to allocate time for reviewing the curriculum and revisiting previous assignments from the group sessions to strengthen their understanding and prepare thoroughly.
Teacher responsible
Additional teachers
| Name | Department | City | |
|---|---|---|---|
| Jesper Grud Skat Madsen | jgsm@bmb.sdu.dk | Institut for Biokemi og Molekylær Biologi | |
| Kumar Somyajit | ksom@sdu.dk | Institut for Biokemi og Molekylær Biologi | |
| Thomas J. D. Jørgensen | tjdj@bmb.sdu.dk | Institut for Biokemi og Molekylær Biologi |
Timetable
Administrative Unit
Team at Registration
Offered in
Recommended course of study
Transition rules
Transitional arrangements describe how a course replaces another course when changes are made to the course of study.
If a transitional arrangement has been made for a course, it will be stated in the list.
See transitional arrangements for all courses at the Faculty of Science.