Module Catalogues, Xi'an Jiaotong-Liverpool University   
Module Code: BIO212
Module Title: Structure and Dynamics of Biomolecules
Module Level: Level 2
Module Credits: 2.50
Academic Year: 2020/21
Semester: SEM2
Originating Department: Biological Sciences
Pre-requisites: N/A
Biomolecules are naturally occurring molecules such as nucleic acids, lipids, sugars and proteins that are essential for normal cellular function. Understanding how these molecules work in terms of their individual architecture and how they interact in cells to form macromolecular ‘machines’ is important to medicine, drug design and bio- and nano-technology. This module aims to provide an introduction to the detailed structure of biomolecules (particularly nucleic acids and proteins), the different techniques used to determine this structure and how structural features define biological function. It will in particular introduce cutting-edge technologies used to investigate protein structure and behaviour from actually visualising molecules using cryo-electron microscopy and X-ray crystallography to determining how molecules move and interact using nuclear magnetic resonance (NMR). The uses, advantages and limitations of these techniques will be illustrated using case studies of specific macromolecular complexes, for example ribosome and ion channels.
Learning outcomes 
On completion of this module students should have acquired a critical understanding of the approaches and methods for studying the structure, function and dynamics of biomolecules. Specifically students should be able to:

A. Explain the key structural features of biomolecules (nucleic acids and proteins) and describe how these features relate to biological function.

B. Discuss how knowledge of biomolecular structure relates to applications in medicine, the pharmaceutical industry and bio- and nano-technology

C. Describe techniques used to determine protein structure and dynamics and discuss the advantages and limitations of each technique

D. Discuss the structural basis of biological processes by describing the structure and function of macromolecular complexes of biomolecules.

Method of teaching and learning 
Module content will be delivered by a combination of lectures and workshops. The contents of lectures (PDF files) are also available on Web. For workshops, each student will need a lap top computer with internet connection.
Block 1: Macromolecular Structure

Lecture 1: Physical and chemical concepts relevant to the main techniques.

Lecture 2 :The forces that hold molecules together. The hydrogen bond, hydrophobic interactions, van der Waals forces, electrostatic interactions. The molecular building blocks. Chemistry of amino acids and nucleotides. The peptide bond. Ramachandran plot. Hierarchical elements in protein structure. The phosphodiester bond. Visualising macromolecule structures.

Lecture 3:Architectural principles of biomolecules. Proteins. Folds; how biological function is defined and supported by the structural features of the molecular building blocks. Domains, supersecondary motifs.

Lecture 4:Molecular structures of ion channels.

Block 2 :Tools of the structural biologist

Lecture 5:X-ray crystallography. Introduction to crystallisation, diffraction, data collection, data analysis (phasing), and model building.

Lecture 6:Nuclear magnetic resonance. NMR spectroscopy is an alternative to X-ray crystallography for analysing small molecules and biological macromolecules in aqueous solution. The basic theory of NMR will be given, showing how a spectrum can be interpreted to give chemical and structural information.

Lecture 7:dditional methods of structural analysis. What if we can not visualise the molecule Alternative methods will be introduced, including electron microscopy, atomic force microscopy, circular dichroism, mass spectrometry, conformational changes monitored with fluorescence and small angle X-ray scattering.

Lecture 8:X-ray crystallography, NMR spectroscopy, and electron microscopy. Practical use of these techniques to understand the structure-function relationship of proteins.

Lecture 9:Bioinformatics based methods.

Lecture 10:Methods to measure the electrophysiological properties of ion channels.

Block 3: Understanding the structural basis of central biological processes

Delivery Hours  
Lectures Seminars Tutorials Lab/Prcaticals Fieldwork / Placement Other(Private study) Total
Hours/Semester 26           49  75 


Sequence Method % of Final Mark
1 Continuous Assessment 15.00
2 Final Exam 85.00

Module Catalogue generated from SITS CUT-OFF: 6/7/2020 4:54:00 AM