BSc Biotechnology / Course details

Year of entry: 2020

Course unit details:
Proteins

Unit code BIOL21111
Credit rating 10
Unit level Level 2
Teaching period(s) Semester 1
Offered by School of Biological Sciences
Available as a free choice unit? No

Overview

Proteins are involved in virtually all biological processes and their structure is key to their function. You will learn how proteins are produced, how they fold into their secondary and tertiary structures and how they interact with each other. You will find out about the experimental techniques, such as X-ray crystallography, nuclear magnetic resonance and electron microscopy, which are used to determine the 3D structure of proteins.

Pre/co-requisites

Unit title Unit code Requirement type Description
Introductory Chemistry BIOL10111 Pre-Requisite Recommended
Biochemistry BIOL10212 Pre-Requisite Compulsory
BIOL21111 Pre & Co-requisites are BIOL10212
  • BIOL10111 Introductory Chemistry (Recommended )

OR

  • CHEM10021/2 Chemistry for Bioscientists 1/2 (Recommended )

Aims

To provide core knowledge of the form, function and role of protein molecules in biological processes and further enable an understanding of biological phenomena at the molecular level.

Learning outcomes

Students will be able to

•       Describe the features of proteins which lead to organelle targeting and subsequent post-translational modification.

•       Describe protein folds in terms of secondary structural elements and the restrictions on peptide structure imposed by the planarity of the peptide bond.

•       Select appropriate experimental techniques for protein purification and characterization (conformation and stability), and describe the relative precision of various approaches and the assumptions implied by each method.

•       Outline methods for 3D structure determination by X-ray crystallography, NMR and electron microscopy.

•       Analyze and manipulate structural data (including the use of the Protein Data Bank in Europe).

•       Analyze data relating to protein function and demonstrate an understanding of associated variables (resolution, Kd, Km & Vmax).

•       Distinguish between various modes of protein-protein interaction and catalysis.

Syllabus

Course material can be divided into three broad themes and will comprise lectures on (1) Protein folding and modification, protein isolation, identification and characterization; (2) Methods for protein structure determination and rational modelling (including an interactive computer workshop); (3) Protein interactions and enzyme characterization.

 eLearning activity

Each of the themes outlined above will be supported by 2 Blackboard eLearning modules each including an online quiz and discussion board. One of the eLearning modules associated with theme (2) will be associated with an interactive computer workshop.

Employability skills

Analytical skills
There is considerable use of graphs and underlying theory in the description of properties of proteins and how these are studied.
Group/team working
Group discussions on the aforementioned boards may be used to supplement private study in groups. A number of in-class exercises are undertaken and additional exercises are provided on the Blackboard site - these can be attempted as group exercises.
Project management
There are regular on line assessments, students must keep pace with the course in order to achieve a good outcome here.
Oral communication
Students ask questions in lectures; interact with teaching staff in 2 microlab workshops and participate in a wrap up Q&A lecture at the end of the course.
Problem solving
Problem solving is developed quite extensively, supported by the on-line exercises; problem driven computer workshops and examples.
Research
There are case study type examples in the course which are directly relevant to research, databases are explored in computer classes which are invaluable in support of research. The emphasis of the course is on practical applications, for example selecting the best technique to address a particular question on protein structure and function.
Written communication
There are discussion boards on Blackboard on specific themes and students are encouraged to use these in support of their studies.
Other
Many of the skills first encountered in the Proteins unit are reinforced in the Biochemistry/Medical Biochemistry semester 4 tutorial program. A large subset of the students therefore extend their skills in smaller teams in tutorials, where they are required to relate and apply the material from Proteins in a problem-solving environment. These thematic tutorials are assessed by the submission of short reports.

Assessment methods

Method Weight
Other 25%
Written exam 75%

2 hour written examination – consisting of essay and/or data interpretation-based questions (75%). Each of the 6 eLearning modules outlined above will contribute to the remaining portion of the assessment (25%).

Feedback methods

Feedback will be provided directly via online discussion boards and through comments in response to practise questions associated with the Blackboard e-learning modules, the mark for assessed Blackboard components is also given as soon as the assignment is completed. Interactive feedback is also provided during the computer workshops at the end of the course. A drop-in session for reviewing marked exam scripts will also be arranged.

Recommended reading

All lecturers provide supporting handouts, the following textbooks may give additional perspectives. Links to Library entries for these are provided within the course Blackboard site.

 

Exploring proteins: a student's guide to experimental skills and methods - Price, Nicholas C., Nairn, Jacqueline 2009

 

Proteins: structure and function - Whitford, David 2003

Study hours

Scheduled activity hours
Assessment written exam 2
Lectures 22
Independent study hours
Independent study 76

Teaching staff

Staff member Role
Stephen Prince Unit coordinator

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