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An advanced treatment of protein science, covering structure, function, applications, and the inter-relationships between these.
The general aim of the course is to introduce students to some of the different techniques used in protein science, and how these are applied to contemporary protein issues.Students will master methods used for studying proteins. They will also be able to use and understand primary scientific publications, and have the ability to independently plan, carry out and critically evaluate experiments.Proteins play an essential role in life, acting as catalysts to speed up chemical reactions, scaffolds that determine cell shape, or signalling molecules that regulate development and responses. In this course we will take an in depth look at the structure and function of proteins, with an emphasis on how understanding the fundamental biochemistry of proteins opens up exciting areas of research. We will explore the methodology used in studying enzymes and the ability to analyse and critically interpret experimental data. The aim is to build a sound understanding of contemporary protein science and an ability to think critically about the current research literature in the field. We will cover a range of issues including protein purification, folding, and aggregation; and the structure, function and evolution of proteins.Recommended preparatory course(s): BIOL 331 / BCHM 301.
As a student in this course, I will develop:A detailed understanding of some of the techniques used in protein science The ability to analyse and critically interpret experimental data and published research.Skills in the verbal and written presentation of scientific ideas.An understanding of the scientific practice and principles of protein science, and an appreciation of why protein science is important in research.An understanding of how protein science methods relates to current protein research.Transferable Skills RegisterAs a student in this course, I will develop the following skills:Experience in analyzing protein science data generated using a variety of methods. There will also be the opportunity to gain experience in carrying out some of these experiments and using the equipment. We will have tutorials looking at the analysis of protein science data, and you will be given the opportunity to analyse novel data.Critical synthesis of information. In everyday life and in many job situations you will be required to read information from different sources, construct your own understanding and shape your own viewpoint. In tutorials we will discuss recent protein science research papers in a group environment and this will develop your abilities to assess the quality of the information, and how methods are applied to research.Generating summaries of protein methods and papers. Clear written and oral communication is essential for most professional careers. As a scientist, it is important to be able to present information clearly and concisely. As part of the work understanding the basis of some protein science methods you will be given feedback on the presentation of this information.Verbal presentation. In most careers in science the ability to present findings clearly in verbal form is likely to be critical. In tutorial sessions we will provide clear guidance on what makes a good presentation and you will test these skills in small group sessions.
Students must attend one activity from each section.
Assumed knowledge What are the different roles that proteins play in the body? What is the basic structure of an amino acid? What functional groups does it contain? If I were to give you a page with the structures of the amino acids, you should be able to recognize and name the different structures. You should also be able to look at the amino acids’ side chains and determine if the amino acid is nonpolar, polar, acidic, or basic. What does the protein “backbone” look like? What is a peptide bond? What kind of a reaction forms a peptide bond? You should be able to draw the resulting dipeptide that forms between two amino acids. You need to know the four different levels of protein structure. What they are and what they are caused by. You should be able to recognize a level of structure from a description of it. What is the difference between alpha helices and beta pleated sheets? What interaction hold secondary structure in place? Which types of interactions hold three dimensional structure in place? Which amino acids are involved in these interactions? You should be able to look at two amino acids and determine which kind of interaction would occur between themIf it has been a while since you have studied proteins, you may want to pick any biochemistry textbook (Garrett & Grisham, Lehinger or any other you can find in the library or lying around), and read the proteins & amino acids chapter.
Professor Borries Demeler, Visiting Erskine Fellow
(University of Lethbridge)
Professor Daniel Bolon, Visiting Erskine Fellow
(University of Massachusetts)
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Domestic fee $1,145.00
International Postgraduate fees
* All fees are inclusive of NZ GST or any equivalent overseas tax, and do not include any programme level discount or additional course-related expenses.
For further information see
School of Biological Sciences