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Protein Crystallography (Postgraduate Certificate using the Internet) - Online

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  • Objectives
    For proper understanding of biological function, the study of the three-dimensional structure of biological macromolecules and their interactions with ligands and the aqueous environment is required. This programme provides an insight into how protein crystal structures are determined and how results should be judged. As a student, you will learn about the fundamentals of protein structure, X-ray diffraction and symmetry; how to determine structure using protein crystallography; and how to assess crystallographic papers and judge the quality of co-ordinates. Additionally, you will complete an independent project based on these skills. This Postgraduate Certificate provides a very good introduction to protein crystallography. It will be of particular benefit to you if you are pursuing a career in this exciting and rapidly expanding field, especially in the pharmaceutical industry, or would like to expand and update your scientific knowledge. It can also form the second year of the MSc Structural Biology using the Internet. The programme is taught entirely using the Internet. After an introduction to effective studying on the Internet, you follow a number of units. As long as you have access to a standard PC or workstation, and an Internet connection, you can undertake this programme from home, work or another university, whether in the UK or abroad.
  • Entry requirements
    Entry requirements Degree in science, computing or mathematics, or equivalent qualification or relevant work experience.
  • Academic Title
    Protein Crystallography (Postgraduate Certificate using the Internet)
  • Course description
    This Postgraduate Certificate is an excellent introduction to protein crystallography. The course is designed for those who are interested in pursuing a career in this exciting and rapidly expanding field, especially in the pharmaceutical industry, or for those who would like to expand and update their existing scientific knowledge.

    The Protein Crystallography course provides an insight into how protein crystal structures are determined and how results should be judged. Up-to-date descriptions of the background, methods and techniques of protein crystallography are explained and the course gives the biologically orientated scientist a mainly non-mathematical insight into how structures are determined and how results should be judged. As a student, you will learn:

    The fundamentals of protein structure
    X-ray diffraction and symmetry
    How to determine structures using protein crystallography
    How to assess crystallographic papers and judge the quality of co-ordinates
    To complete an independent project based on these skills
    Distance learning course

    PX is a distance learning course. All teaching is carried out via the internet. The only equipment required is a standard PC or workstation and an Internet connection.

    Modular structure

    PX may be taken as a stand-alone postgraduate certificate or as part of the School of Crystallography's innovative distance learning MSc in Structural Molecular Biology.

    The programme of study has a modular structure and operates under the Birkbeck Common Awards Scheme, one module being worth 30 credits. Students gain 60 credits on completion of the PX Postgraduate Certificate. In order to gain an MSc in Structural Molecular Biology students must earn 180 credits.

    Protein crystallography is no longer solely the domain of the mathematician and physicist, but that of the biologically orientated scientist. It is a multidisciplinary technique which overlaps with biochemistry, molecular biology, bioinformatics, biophysics and organic chemistry.

    For proper understanding of biological function a detailed knowledge of the three-dimensional structure of biological macromolecules and their interactions with ligands and the aqueous environment is required.

    Protein crystallography
    (or structural molecular biology) is powerful in that it can identify the residues determining substrate specificity and interactions with other macromolecules at the atomic level, allowing the targeting of site-directed mutagenesis experiments and the design of selective inhibitors, so important in industry.

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