General Information
Medical Biochemistry 1 has been specifically designed to build on students' knowledge of chemistry as preparation for the more specialised field of biochemistry. The over-arching learning theme is to gain an in-depth knowledge of biomolecular structure and the structure/function relationship of biomolecules. A modern teaching style is applied to accommodate varied learning styles and combines forums, narrated powerpoints, screencasts and group learning sessions. Key learning outcomes are facilitated in a technology-enhanced environment to enhance understanding, including problem-based learning and a molecular modelling assignment. Students will gain a detailed understanding of buffer systems, enzyme kinetics, regulation and mechanisms as well as key intracellular signalling cascades. The subject incorporates biochemical laboratory techniques such as a number of chromatography and spectroscopy techniques.
-
Details
Academic unit: Faculty of Health Sciences and Medicine Subject code: BMED11-205 Subject title: Medical Biochemistry 1 Subject level: Undergraduate Semester/Year: January 2025 Credit points: 10.000 -
Delivery & attendance
Timetable: https://bond.edu.au/timetable Delivery mode: Standard Workload items: - Forum: x12 (Total hours: 24) - Forum
- Group Learning: x12 (Total hours: 12) - Group Learning
- Tutorial: x12 (Total hours: 24) - Tutorial
- Science Lab: x5 (Total hours: 15) - Science Lab
- Personal Study Hours: x12 (Total hours: 45) - Personal study
Attendance and learning activities: Attendance at all tutorials and practical laboratory sessions is expected. Attendance in tutorials and labs will be recorded and monitored. Students who are unable to attend due to illness must provide a valid medical certificate. This subject is designed to integrate forums (2 hours per week), tutorials (2 hours per week), and practical laboratory sessions. Content delivered each week in these sessions build on (& complement) the work of the previous ones and it is difficult to recover if you miss a session. -
Resources
Prescribed resources: No Prescribed resources.
After enrolment, students can check the Books and Tools area in iLearn for the full Resource List.iLearn@Bond & Email: iLearn@Bond is the Learning Management System at Bond University and is used to provide access to subject materials, class recordings and detailed subject information regarding the subject curriculum, assessment, and timing. Both iLearn and the Student Email facility are used to provide important subject notifications.
Additionally, official correspondence from the University will be forwarded to students’ Bond email account and must be monitored by the student.
To access these services, log on to the Student Portal from the Bond University website as www.bond.edu.au
| Academic unit: | Faculty of Health Sciences and Medicine |
|---|---|
| Subject code: | BMED11-205 |
| Subject title: | Medical Biochemistry 1 |
| Subject level: | Undergraduate |
| Semester/Year: | January 2025 |
| Credit points: | 10.000 |
| Timetable: | https://bond.edu.au/timetable |
|---|---|
| Delivery mode: | Standard |
| Workload items: |
|
| Attendance and learning activities: | Attendance at all tutorials and practical laboratory sessions is expected. Attendance in tutorials and labs will be recorded and monitored. Students who are unable to attend due to illness must provide a valid medical certificate. This subject is designed to integrate forums (2 hours per week), tutorials (2 hours per week), and practical laboratory sessions. Content delivered each week in these sessions build on (& complement) the work of the previous ones and it is difficult to recover if you miss a session. |
| Prescribed resources: | No Prescribed resources. After enrolment, students can check the Books and Tools area in iLearn for the full Resource List. |
|---|---|
| iLearn@Bond & Email: | iLearn@Bond is the Learning Management System at Bond University and is used to provide access to subject materials, class recordings and detailed subject information regarding the subject curriculum, assessment, and timing. Both iLearn and the Student Email facility are used to provide important subject notifications. Additionally, official correspondence from the University will be forwarded to students’ Bond email account and must be monitored by the student. To access these services, log on to the Student Portal from the Bond University website as www.bond.edu.au |
Enrolment requirements
| Requisites: |
Pre-requisites:Co-requisites:There are no co-requisites |
|---|---|
| Assumed knowledge: |
Assumed knowledge is the minimum level of knowledge of a subject area that students are assumed to have acquired through previous study. It is the responsibility of students to ensure they meet the assumed knowledge expectations of the subject. Students who do not possess this prior knowledge are strongly recommended against enrolling and do so at their own risk. No concessions will be made for students’ lack of prior knowledge.
|
| Restrictions: |
Nil |
Assurance of learning
Assurance of Learning means that universities take responsibility for creating, monitoring and updating curriculum, teaching and assessment so that students graduate with the knowledge, skills and attributes they need for employability and/or further study.
At Bond University, we carefully develop subject and program outcomes to ensure that student learning in each subject contributes to the whole student experience. Students are encouraged to carefully read and consider subject and program outcomes as combined elements.
Program Learning Outcomes (PLOs)
Program Learning Outcomes provide a broad and measurable set of standards that incorporate a range of knowledge and skills that will be achieved on completion of the program. If you are undertaking this subject as part of a degree program, you should refer to the relevant degree program outcomes and graduate attributes as they relate to this subject.
Subject Learning Outcomes (SLOs)
On successful completion of this subject the learner will be able to:
- Describe the structure of biomolecules and the key chemical concepts that underpin biomolecular structures and relate their function to the important and relevant aspects of their structure.
- Solve and explain biochemical questions relating to the biomolecular structure-function relationship and solve acid-base and enzyme kinetics problems using quantitative methods.
- Locate, use and interpret information and data relating to various chemical topics.
- Explain molecular mechanisms in a number of important cell signalling cascades.
- Critically appraise and apply scientific literature in the medical biochemistry field to the understanding of pharmaceutical action, which fosters innovation in scientific research.
- Communicate effectively using appropriate conventions and language relevant to biochemistry.
- Competently perform advanced biochemical techniques including chromatography, spectrophotometry and electrophoresis.
- Understand key features of biomolecules and intracellular signalling systems which underpin universal health and reduce preventable deaths to ensure healthy lives while promoting well-being for all at all ages.
Generative Artificial Intelligence in Assessment
The University acknowledges that Generative Artificial Intelligence (Gen-AI) tools are an important facet of contemporary life. Their use in assessment is considered in line with students’ development of the skills and knowledge which demonstrate learning outcomes and underpin study and career success. Instructions on the use of Gen-AI are given for each assessment task; it is your responsibility to adhere to these instructions.
-
Assessment details
Type Task % Timing* Outcomes assessed Computer-Aided Examination (Closed) End of semester exam 40.00% Final Examination Period 1,2,3,4,5,8 Computer-aided Test (Closed) Test 20.00% Week 6 1,2,3,4,5 Laboratory Report Laboratory report 25.00% Week 9 1,3,4,5,6,7,8 Assignment§ Group Research-based Assignment conducted over the semester. Presentation at the end of semester. 15.00% Week 11 1,2,3,4,5,6 - § Indicates group/teamwork-based assessment
- * Assessment timing is indicative of the week that the assessment is due or begins (where conducted over multiple weeks), and is based on the standard University academic calendar
- C = Students must reach a level of competency to successfully complete this assessment.
-
Assessment criteria
Assessment criteria
High Distinction 85-100 Outstanding or exemplary performance in the following areas: interpretative ability; intellectual initiative in response to questions; mastery of the skills required by the subject, general levels of knowledge and analytic ability or clear thinking. Distinction 75-84 Usually awarded to students whose performance goes well beyond the minimum requirements set for tasks required in assessment, and who perform well in most of the above areas. Credit 65-74 Usually awarded to students whose performance is considered to go beyond the minimum requirements for work set for assessment. Assessable work is typically characterised by a strong performance in some of the capacities listed above. Pass 50-64 Usually awarded to students whose performance meets the requirements set for work provided for assessment. Fail 0-49 Usually awarded to students whose performance is not considered to meet the minimum requirements set for particular tasks. The fail grade may be a result of insufficient preparation, of inattention to assignment guidelines or lack of academic ability. A frequent cause of failure is lack of attention to subject or assignment guidelines. Quality assurance
For the purposes of quality assurance, Bond University conducts an evaluation process to measure and document student assessment as evidence of the extent to which program and subject learning outcomes are achieved. Some examples of student work will be retained for potential research and quality auditing purposes only. Any student work used will be treated confidentially and no student grades will be affected.
| Type | Task | % | Timing* | Outcomes assessed |
|---|---|---|---|---|
| Computer-Aided Examination (Closed) | End of semester exam | 40.00% | Final Examination Period | 1,2,3,4,5,8 |
| Computer-aided Test (Closed) | Test | 20.00% | Week 6 | 1,2,3,4,5 |
| Laboratory Report | Laboratory report | 25.00% | Week 9 | 1,3,4,5,6,7,8 |
| Assignment§ | Group Research-based Assignment conducted over the semester. Presentation at the end of semester. | 15.00% | Week 11 | 1,2,3,4,5,6 |
- § Indicates group/teamwork-based assessment
- * Assessment timing is indicative of the week that the assessment is due or begins (where conducted over multiple weeks), and is based on the standard University academic calendar
- C = Students must reach a level of competency to successfully complete this assessment.
Assessment criteria
| High Distinction | 85-100 | Outstanding or exemplary performance in the following areas: interpretative ability; intellectual initiative in response to questions; mastery of the skills required by the subject, general levels of knowledge and analytic ability or clear thinking. |
|---|---|---|
| Distinction | 75-84 | Usually awarded to students whose performance goes well beyond the minimum requirements set for tasks required in assessment, and who perform well in most of the above areas. |
| Credit | 65-74 | Usually awarded to students whose performance is considered to go beyond the minimum requirements for work set for assessment. Assessable work is typically characterised by a strong performance in some of the capacities listed above. |
| Pass | 50-64 | Usually awarded to students whose performance meets the requirements set for work provided for assessment. |
| Fail | 0-49 | Usually awarded to students whose performance is not considered to meet the minimum requirements set for particular tasks. The fail grade may be a result of insufficient preparation, of inattention to assignment guidelines or lack of academic ability. A frequent cause of failure is lack of attention to subject or assignment guidelines. |
Quality assurance
For the purposes of quality assurance, Bond University conducts an evaluation process to measure and document student assessment as evidence of the extent to which program and subject learning outcomes are achieved. Some examples of student work will be retained for potential research and quality auditing purposes only. Any student work used will be treated confidentially and no student grades will be affected.
Study Information
Submission procedures
Students must check the iLearn@Bond subject site for detailed assessment information and submission procedures.
Policy on late submission and extensions
A late penalty will be applied to all overdue assessment tasks unless an extension is granted by the subject coordinator. The standard penalty will be 10% of marks awarded to that assessment per day late with no assessment to be accepted seven days after the due date. Where a student is granted an extension, the penalty of 10% per day late starts from the new due date.
Academic Integrity
Bond University‘s Student Code of Conduct Policy , Student Charter, Academic Integrity Policy and our Graduate Attributes guide expectations regarding student behaviour, their rights and responsibilities. Information on these topics can be found on our Academic Integrity webpage recognising that academic integrity involves demonstrating the principles of integrity (honesty, fairness, trust, professionalism, courage, responsibility, and respect) in words and actions across all aspects of academic endeavour.
Staff are required to report suspected misconduct. This includes all types of plagiarism, cheating, collusion, fabrication or falsification of data/content or other misconduct relating to assessment such as the falsification of medical certificates for assessment extensions. The longer term personal, social and financial consequences of misconduct can be severe, so please ask for help if you are unsure.
If your work is subject to an inquiry, you will be given an opportunity to respond and appropriate support will be provided. Academic work under inquiry will not be marked until the process has concluded. Penalties for misconduct include a warning, reduced grade, a requirement to repeat the assessment, suspension or expulsion from the University.
Feedback on assessment
Feedback on assessment will be provided to students according to the requirements of the Assessment Procedure Schedule A - Assessment Communication Procedure.
Whilst in most cases feedback should be provided within two weeks of the assessment submission due date, the Procedure should be checked if the assessment is linked to others or if the subject is a non-standard (e.g., intensive) subject.
Accessibility and Inclusion Support
Support is available to students where a physical, mental or neurological condition exists that would impact the student’s capacity to complete studies, exams or assessment tasks. For effective support, special requirement needs should be arranged with the University in advance of or at the start of each semester, or, for acute conditions, as soon as practicable after the condition arises. Reasonable adjustments are not guaranteed where applications are submitted late in the semester (for example, when lodged just prior to critical assessment and examination dates).
As outlined in the Accessibility and Inclusion Policy, to qualify for support, students must meet certain criteria. Students are also required to meet with the Accessibility and Inclusion Advisor who will ensure that reasonable adjustments are afforded to qualifying students.
For more information and to apply online, visit BondAbility.
Additional subject information
Subject curriculum
-
1 - Introduction to Biochemistry
During this Introduction, we discover the underlying, organizing biochemical principle shared by living systems; give a structural overview of the major biomolecules, revise some key chemical concepts; emphasize the importance of and explain the difference between various types of isomers; describe key laboratory techniques relevant biochemistry.
SLOs included
- Describe the structure of biomolecules and the key chemical concepts that underpin biomolecular structures and relate their function to the important and relevant aspects of their structure.
- Locate, use and interpret information and data relating to various chemical topics.
- Competently perform advanced biochemical techniques including chromatography, spectrophotometry and electrophoresis.
-
2- Water and Buffers
We explore the importance of water in biological systems (structure/role/special properties/colligative properties) revise key chemical concepts of non-covalent bonding and consider their importance in a biological context. Next we delve into the behaviour of weak acids/bases; how buffers work, solve buffer problems using the Henderson-Hasselbach equation & Le Chatelier's principle. Finally we focus on important body buffer systems.
-
3. Protein structure
A detailed exploration into all levels of protein structure hierarchy is provided: amino acid classification, enantiomer determination; acid-base nature of amino acids/peptides & proteins. Also explored is the structural biology of phi/psi dihedral angles and their significance to protein structure, explore factors that stabilise 3D structure Of proteins; motifs/domains. Finally we explore protein folding and pathologies associated with errors in folding (amyloidosis).
SLOs included
- Describe the structure of biomolecules and the key chemical concepts that underpin biomolecular structures and relate their function to the important and relevant aspects of their structure.
- Solve and explain biochemical questions relating to the biomolecular structure-function relationship and solve acid-base and enzyme kinetics problems using quantitative methods.
- Locate, use and interpret information and data relating to various chemical topics.
- Understand key features of biomolecules and intracellular signalling systems which underpin universal health and reduce preventable deaths to ensure healthy lives while promoting well-being for all at all ages.
-
4. Protein Structure Function Relationship
This section describes key features of protein function such as reversible binding, specificity etc. Detailed examples of the protein structure-function relationship are provided, in particular, oxygen-binding proteins and immunoglobulins are highlighted. A range of medical examples are included.
SLOs included
- Describe the structure of biomolecules and the key chemical concepts that underpin biomolecular structures and relate their function to the important and relevant aspects of their structure.
- Solve and explain biochemical questions relating to the biomolecular structure-function relationship and solve acid-base and enzyme kinetics problems using quantitative methods.
- Locate, use and interpret information and data relating to various chemical topics.
- Understand key features of biomolecules and intracellular signalling systems which underpin universal health and reduce preventable deaths to ensure healthy lives while promoting well-being for all at all ages.
-
5. Enzymes
In this Topic we extend our knowledge of the previous topic specifically to enzymes; a quantitative look at enzyme function; kinetics (Michaelis-Menten); problem solving using M-M equation. Then we consider the importance of regulation of activity through examples of various types of inhibition/activiation and how we may measure them.
-
6. Carbohydrates
Here we provide a detailed treatment of carbohydrate structure, hierarchy, physical and chemical properties, nomenclature. There is an emphasis on understanding and ability to draw the basic monosaccharide structure and how glycosidic bonds are formed. We provide examples of the important roles of carbohydrates in biological systems.
-
7. Amino Acids, Peptides and Proteins
Basic structure of amino acids; key chemical and physical properties of their side chains, peptide bonds, drawing peptides, acid-base properties of amino acids, peptides and proteins, hierarchy of protein strucure; isoelectric point, weak acid/.base titration graphs. Next we focus on the nature of ligand binding to proteins (qualitiative & quantitative), governing principles (thermodynamic/entropic considerations); the over-arching theme of protein structure-function relationship; medical applications and pathologies associated with this topic.
-
8. Intracellular Signalling
The capstone topic for this subject is developing an understanding at the molecular level, of how chemical signals can transmit their messages intracellularly. We provide detailed examples of G-protein coupled receptors and receptor tyrosine kinase systems in the context of the more broader 'whole body' fasting and fed state scenarios respectively. This will provide a great basis from which to begin Medical Biochemistry 2 next semester.