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 lectures, 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.
|Academic unit:||Faculty of Health Sciences and Medicine|
|Subject title:||Medical Biochemistry 1|
Delivery & attendance
|Attendance and learning activities:||Attendance at tutorials is compulsory. Students are required to attend a minimum of 75% of the tutorials and submit worksheets from the tutorial each week in order to pass the subject.|
|Prescribed resources:|| |
|[email protected] & Email:||[email protected] is the online learning environment at Bond University and is used to provide access to subject materials, lecture 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
There are no co-requisites.
This subject is not available as a general elective. To be eligible for enrolment, the subject must be specified in the students’ program structure.
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 scientific literature in the medical biochemistry field.
- Communicate effectively using appropriate conventions and language relevant to biochemistry.
- Competently perform advanced biochemical techniques including chromatography, spectrophotometry and electrophoresis.
|Laboratory Activity||Laboratory activity||30%||Ongoing||1, 2, 3, 4, 5, 6, 7.|
|Online Quiz||Test - topic 1 and 2||15%||Week 5||1, 2, 3, 4, 5.|
|Online Quiz||Test - Topic 3 and 4||15%||Week 9||1, 2, 3, 4, 5.|
|Essay §||Assignment||10%||In Consultation||1, 2, 3, 4, 5, 6.|
|Computer-Aided Examination (Closed)||End of semester exam||30%||Final Examination Period||1, 2, 3, 4, 5.|
Students must gain a pass or higher in the End of Semester examination in order to pass the overall subject. This is because this subject is a prerequisite to Medical Biochemistry 2 which assumes a certain level of prior knowledge.
- § 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.
|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.|
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.
Students must check the [email protected] 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.
Policy on plagiarism
University’s Academic Integrity Policy defines plagiarism as the act of misrepresenting as one’s own original work: another’s ideas, interpretations, words, or creative works; and/or one’s own previous ideas, interpretations, words, or creative work without acknowledging that it was used previously (i.e., self-plagiarism). The University considers the act of plagiarising to be a breach of the Student Conduct Code and, therefore, subject to the Discipline Regulations which provide for a range of penalties including the reduction of marks or grades, fines and suspension from the University.
Feedback on assessment
Feedback on assessment will be provided to students within two weeks of the assessment submission due date, as per the Assessment Policy.
If you have a disability, illness, injury or health condition that impacts your capacity to complete studies, exams or assessment tasks, it is important you let us know your special requirements, early in the semester. Students will need to make an application for support and submit it with recent, comprehensive documentation at an appointment with a Disability Officer. Students with a disability are encouraged to contact the Disability Office at the earliest possible time, to meet staff and learn about the services available to meet your specific needs. Please note that late notification or failure to disclose your disability can be to your disadvantage as the University cannot guarantee support under such circumstances.
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.1, 3, 7.
We explore the importance of water in biological systems (structure/role/special properties/colligative properties) revise key chemical concepts ot non-covalent bonding & 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.1, 2, 3.
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 topic1, 2, 5.
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.1, 2, 3, 5, 7.
Here we provide a detailed treatment of carbohydrate structure, hierarchy, physical & chemical properties, nomenclature. There is an emphasis on understanding & ability to draw the basic monosaccharide structure & how glycosidic bonds are formed. We provide examples of important roles of carbohydrates in biological systems.1, 3.
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,1, 3, 4.