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:

  • Have a basic knowledge of physics, chemistry and biology
  • Be able to use a computer and access the internet
  • Have previous experience in laboratory work
  • 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.

    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

    86 hours per semester

    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

    Name E-mail Department
    Lars Grøntved larsgr@bmb.sdu.dk Institut for Biokemi og Molekylær Biologi

    Additional teachers

    Name E-mail 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

    Biokemi og Molekylær Biologi

    Team at Registration

    NAT

    Offered in

    Odense

    Recommended course of study

    Profile Education Semester Offer period

    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.