Protein Structure and Function
This page was last updated on 22/07/2015.
In contrast to what you might have been expecting from previous biochemistry papers such as BIOSCI 106 and BIOSCI 203, BIOSCI 350: Protein Structure and Function will not be teaching you about how alpha-helices and beta-sheets are chemically arranged. Instead, this course is focused on delivering content based around how practical laboratory techniques are used to find out, manipulate and solve protein structures.
This paper has 4 lecturers in total: Dr. Richard Kingston, Professor Tom Brittain, your course-coordinator Dr. Chris Squire, and Associate Professor Alok Mitra. Each lecturer takes a section that comprises of 9-10 lectures and there are a few topics that overlap between each. The mid-semester test has questions from the first half of lectures (Dr. Kingston and Professor Brittain) and the end-of-semester test tests the second half (Dr. Squire and Associate Professor Mitra), while the exam covers content taught during the entire semester. Each lecturer gave you two questions to choose from in the test and exam, with the exception of Associate Professor Mitra who wrote out three compulsory short-answer questions.
In 2015 the first three laboratories were taken by Dr. Richard Kingston, and are unlike the typical undergraduate laboratories you would have done up to this stage where you were given instructions to follow, perform an experiment and complete a lab worksheet to hand in. Instead, you were to carry out some authentic scientific research via basic experimentation to help characterize the the proteins involved in the replication of Wobbly Possum Disease Virus (WPDV) in which the outcomes were not completely known. Don't freak out - you will still be given very detailed instructions on how to go about performing the in-lab experiments but be wary that that post-lab questions will require you to think critically and show understanding about what you did during the lab - as always, make sure to ask lots of questions before you leave the lab to clear up any confusions as his questions can be tricky. Note, 2015 was the first year in which this sort of lab took place. For the lab reports, Kingston provided us with lab report outlines which contained all the questions which offered a bit more guidance.
In Dr. Chris Squire's lab - which in 2015 was a dry lab meaning you did not need a lab coat - you were to use a computer software to learn to visualize electron density, fit a mutant enzyme to an experimental electron density, build and fit a molecule of Tamiflu into the electron density map and finally discuss the mechanism of drug resistance. In one of his lectures he will actually briefly show you how to do this live, but don't be surprised if you find yourself struggling on the day - a lot of the time your progress may be stalled not because you don't know what to do but how to get the software to do it, so please ask the ever-helpful demonstrators for their expertise. The assignment sheet for this lab contains simple and straightforward questions, but make sure your Tamiflu molecule drawing contains the appropriate amount of detail required or you could lose easy marks here.
In the final laboratory with Associate Professor Mitra, he will spend most of it showing you diffraction patterns and explaining the relationship between images and their diffraction patterns - make sure you pay close attention to this as this knowledge is critical to the post-lab online quiz on CECIL, where you will match a set of images to their optical diffraction patterns jumbled in random order. There was a lot of confusion amongst my friends in regards to the correct answer, so if you are certain in your answers don't be afraid to do the quiz as you see fit. It goes without saying that playing with the computer program in class and asking the demonstrators will help you immensely for this task.
Overall, the laboratory component of BIOSCI 350 is not extremely difficult, but it is the little mistakes which can cost you so be careful, be diligent and ask lots and lots (and lots!!) of questions!!
Proteins: Purification & Analysis
Dr. Richard Kingston's lectures in 2015 were based around three broad topics:
Protein actions and Interactions
Professor Tom Brittain was up next, and his lectures covered seven topics:
Protein Structure Determination, Evolution and Drug Discovery
The very funny and entertaining Dr. Chris Squire kicked off the second half of the course - a note here that he does very hilarious demonstrations in class and cracks wicked jokes, so you do not want to miss his lectures. His module covered the following topics:
Finishing off the course is Associate Professor Alok Mitra, who covered the following eight topics: