BSc Microbiology with a Modern Language

Year of entry: 2024

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Course unit details:
Proteins

Course unit fact file
Unit code	BIOL21111
Credit rating	10
Unit level	Level 2
Teaching period(s)	Semester 1
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
Biochemistry	BIOL10212	Pre-Requisite	Compulsory
Chemistry for Bioscientists 1	CHEM10021	Pre-Requisite	Recommended
Chemistry for Bioscientists 2	CHEM10022	Pre-Requisite	Recommended

BIOL21111 Pre-requisite is BIOL10212

BIOL10111 Introductory Chemistry (Recommended )

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

Lecture Content
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; (3) Protein interactions and enzyme characterization.

eLearning Activity
Each of the themes outlined above will be supported by Blackboard eLearning modules each including an online quiz and discussion board.

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%

Two hour written examination 1 integrative essay question (including data interpretation) from a choice of 2 (75%). Each of the 5 eLearning modules outlined above will contribute to the remaining portion of the assessment (5% each).

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.

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

Additional notes

Students MUST take one of recommended pre-requisite CHEM10021 OR CHEM10022

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.

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