Module Specification
The information contained in this module specification was correct at the time of publication but may be subject to change, either during the session because of unforeseen circumstances, or following review of the module at the end of the session. Queries about the module should be directed to the member of staff with responsibility for the module.
Title Protein Structure, Function and Organisation
Code LIFE303
Coordinator Prof L Lian
Biochemistry
Lu-Yun.Lian@liverpool.ac.uk
Year CATS Level Semester CATS Value
Session 2017-18 Level 6 FHEQ First Semester 15

Pre-requisites before taking this module (other modules and/or general educational/academic requirements):
LIFE203  

Modules for which this module is a pre-requisite:
 

Co-requisite modules:
 

Linked Modules:
 

Teaching Schedule
  Lectures Seminars Tutorials Lab Practicals Fieldwork Placement Other TOTAL
Study Hours 22
Timetabled lectures to introduce key concepts
        1
This is a timetabled bioinformatics workshop
23
Timetable (if known)              
Private Study 127
TOTAL HOURS 150

Assessment
EXAM Duration Timing
(Semester)		 % of
final
mark		 Resit/resubmission
opportunity		 Penalty for late
submission		 Notes
Unseen Written Exam  120  Semester 1  70  Yes    Final exam 
Unseen Written Exam  2 hrs  Semester 1  30  Yes    In-class tests Notes (applying to all assessments) Assessment 1 will be a written examination consisting of two extended pieces of writing (short essays and data interpretation/ analysis). Assessment 2 will be 2 written assignments of equal weighting, written under examination conditions, consisting of short answer questions. The first test will take place around week 3 and feedback will be provided in time for the second test which takes place towards the end of the module. The marks for the two in-class tests will  
CONTINUOUS Duration Timing
(Semester)		 % of
final
mark		 Resit/resubmission
opportunity		 Penalty for late
submission		 Notes
             

Aims

  1. To develop in students knowledge and understanding why protein structures are important for function, and how proteins fold into functional conformations

  2. To provide an overview of current NMR, X-ray crystallography and proteomics-based approaches to solve fundamental and applied problems in biology and biotechnology

  3. To explain to students the latest techniques used to define protein structures

Learning Outcomes

To describe in detail, current methods used for the determination and analysis of protein structures

To critically discuss how proteomics-based approaches can be used to study fundamental and applied biological problems

To discuss the latest methods of analysis of post-translational modifications of proteins and implications for cell function

To critically evaluate the strengths and weakness of the different technologies - nuclear magnetic resonance (NMR), x-ray crystallography- mass spectrometry  and how they can be used in an integrated manner

To discuss the prerequisites for obtaining structures such as protein foldedness and sample preparations

Teaching and Learning Strategies

Lecture - Timetabled lectures to introduce key concepts

Workshop - This is a timetabled bioinformatics workshop

Syllabus
1 

Methods of proteome analysis: Revision of protein structure. Primary structure and amino acid modifications.

 
Identification of proteins from primary structure: Use of molecular mass of proteins and peptides to determine amino acid composition and sequence.
 
Basic proteomic methods: Basics of mass spectrometry.
 
Applications of proteomic techniques: Use in human and microbes.
 
Applications of proteomic techniques: Subcellular proteomics. Post-translational modifications.
 
< div style="line-height:150%;margin:0cm 0cm 0pt" xmlns="http://www.w3.org/1999/xhtml">Acquisition of protein structure: Protein folding in vivo and in vitro
 
Bringing together the techniques of structural biology: Overview of techniques and applications
 
Recombinant Protein Production: Methods for making recombinant proteins and purification
 
Nuclear magnetic resonance: Structural determination. Molecula r dynamics & interactions
 
X-ray crystallography: X-ray crystallography. Applications
 
Advanced methods: Synchrotron-based structural methods for structure determination of proteins.
 
A case study: Molecular motors and N-acetylcholine receptors

Recommended Texts
Reading lists are managed at readinglists.liverpool.ac.uk. Click here to access the reading lists for this module.
Explanation of Reading List:

Students will be directed to current primary research articles.