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Overview

Molecular machines and protein complexes. How the atomic structures of proteins dictate function, reflect diversity and guide bioengineering. Design of novel proteins and drugs. Proteome and protein structure analysis.

The diverse enzymatic activities and interactions of proteins underpin all life on our planet. The atomic resolution structures of proteins provide profound insights into protein function, its evolution and how it can be manipulated in medicine and biotechnology. BIOC 351 focuses on these aspects of protein biochemistry and uses selected examples from research articles to illustrate how deep, fundamental understanding is achieved. With a strong emphasis on the experimental basis of biochemistry, BIOC 351 will prepare students for employment in jobs based on laboratory science or on the knowledge it generates. In addition, the paper emphasises skills that are crucial for success during postgraduate study in many life sciences.

About this paper

Paper title Advanced Protein Biochemistry
Subject Biochemistry
EFTS 0.15
Points 18 points
Teaching period Semester 1 (On campus)
Domestic Tuition Fees ( NZD ) $1,318.20
International Tuition Fees Tuition Fees for international students are elsewhere on this website.
Prerequisite
BIOC 221 and BIOC 222
Schedule C
Science
Notes
In approved cases another 200-level science paper may be substituted for BIOC 221.
Eligibility

This paper is suitable for students in any discipline who have an interest in protein structure and function.

Contact
biochem300.tf@otago.ac.nz
Teaching staff

Convenor: Professor Catherine Day and Dr Ben Peters

Paper Structure

Lectures are held twice a week for the semester with a third lecture per week for half of the semester.

Labs are held once a week per stream for five weeks.

Teaching Arrangements

Arrangements can be made for students to leave the lab for other commitments such as lectures and are able to plan their laboratory experiments to fit in with those commitments.

Textbooks
Voet, D., Voet, J. G., and Pratt, C. W. Fundamentals of Biochemistry, John Wiley & Sons.
Graduate Attributes Emphasised
Lifelong learning, Scholarship, Critical thinking, Research, Self-motivation.
View more information about Otago's graduate attributes.
Learning Outcomes

Students who successfully complete this paper will:

  • Articulate a detailed understanding of protein structure, molecular interactions and how these features define the functions of enzymes and signaling molecules
  • Identify and critically evaluate relevant information about protein structure, function and engineering in primary sources and authoritative databases
  • Critically assess experimental data from X-ray crystallography, mass spectrometry, and other biophysical techniques
  • Understand the relationship between hypothesis, experimental design and data and know how to apply this to attain knowledge
  • Design and execute experiments using contemporary biochemical techniques
Assessment details

30% Internal assessments

70% Final examination

Timetable

Semester 1

Location
Dunedin
Teaching method
This paper is taught On Campus
Learning management system
Aoroa

Lecture

Stream Days Times Weeks
Attend
A1 Monday 10:00-10:50 16-17, 19, 21
Tuesday 10:00-10:50 9-14, 16-22
Wednesday 10:00-10:50 9-14, 16-22

Practical

Stream Days Times Weeks
Attend one stream from
A1 Thursday 09:00-09:50 16-21
Thursday 11:00-17:50 16-21
A2 Tuesday 09:00-09:50 16-21
Tuesday 11:00-17:50 16-21

Workshop

Stream Days Times Weeks
Attend one stream from
A1 Wednesday 12:00-13:50 11-12
A2 Wednesday 15:00-16:50 11-12

Overview

Molecular machines and protein complexes. How the atomic structures of proteins dictate function, reflect diversity, and guide bioengineering. Design of novel proteins and drugs. Proteome and protein structure analysis.

Protein structure and dynamics underpin biological function and are central to understanding cellular processes. This paper examines how conformational changes drive catalysis, regulation and molecular recognition. Students explore modern structural approaches, including X-ray crystallography, NMR spectroscopy and cryoEM, alongside computational methods such as AlphaFold.

BIOC 351 also introduces the principles of protein engineering and de novo design, and demonstrates how structural information enables structure-based drug discovery. Using real structural data and case studies, students develop critical skills in analysing protein structures and applying this knowledge to problems in health, disease and biotechnology.

About this paper

Paper title Advanced Protein Technology
Subject Biochemistry
EFTS 0.15
Points 18 points
Teaching period Semester 1 (On campus)
Domestic Tuition Fees Tuition Fees for 2027 have not yet been set
International Tuition Fees Tuition Fees for international students are elsewhere on this website.
Prerequisite
BIOC 222
Schedule C
Science
Eligibility

This paper is suitable for students in any discipline who have an interest in protein structure and function.

Contact
biochem300.tf@otago.ac.nz
Teaching staff

Conveners:

  • Professor Catherine Day
  • Dr Ben Peters
  • Paper Structure
  • Lectures are held twice a week for the semester.
  • Labs are held once a week for six weeks in the second half of semester.
  • Two tutorials and three lab lectures complement the laboratory classes.
  • Teaching Arrangements

    Arrangements can be made for students to leave the lab for one hour to attend other classes.

    Textbooks

    Textbooks are not required for this paper.

    Graduate Attributes Emphasised
    Lifelong learning, Scholarship, Critical thinking, Research, Self-motivation.
    View more information about Otago's graduate attributes.
    Learning Outcomes

    Students who successfully complete this paper will:

    • Articulate a detailed understanding of protein structure, molecular interactions and how these features define the functions of enzymes and signaling molecules.
    • Identify and critically evaluate relevant information about protein structure, function and engineering in primary sources and authoritative databases.
    • Critically assess experimental data from X-ray crystallography, mass spectrometry and other biophysical techniques.
    • Understand the relationship between hypothesis, experimental design and data and know how to apply this to attain knowledge.
    • Design and execute experiments using contemporary biochemical techniques.
    Assessment details
  • Internal assessments (30%)
  • Final examination (70%)
  • Timetable

    Semester 1

    Location
    Dunedin
    Teaching method
    This paper is taught On Campus
    Learning management system
    Aoroa

    Lecture

    Stream Days Times Weeks
    Attend
    A1 Tuesday 10:00-10:50 9-12, 15-22
    Wednesday 10:00-10:50 9-12, 15-22
    AND
    B1 Monday 10:00-10:50 15-16, 18-20

    Practical

    Stream Days Times Weeks
    Attend one stream from
    A1 Thursday 09:00-09:50 17-21
    Thursday 11:00-17:50 17-21
    A2 Tuesday 09:00-09:50 17-21
    Tuesday 11:00-17:50 17-21

    Workshop

    Stream Days Times Weeks
    Attend one stream from
    A1 Friday 15:00-16:50 15-16
    A2 Monday 15:00-16:50 15-16
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