Available online
Description
Probing proteins -- This selection looks at the two main techniques for studying protein structure. With crystals as the starting point, X ray diffraction can give 3-dimensional information in atom...ic detail. For molecules in solution, nuclear magnetic resonance, or NMR, is the method of choice. What are the strengths and limitations of these techniques and in what way might they provide complementary information? One protein that has been studied in detail by both methods is the enzyme, BARNASE. This band will show the model of BARNASE that has emerged from these studies and the insights it has given about how the molecule functions. -- Molecules on the move -- The first section looks at how molecular motion in barnase has been modelled on computer graphics. what role might this dynamic behaviour play in protein function. the second section deals with another puzzle. How do proteins, built from a linear string of amino acids, fold into a 3 dimensional conformation that's both unique and biologically active? The problem of protein folding in barnase has been tackled by a combination of protein engineering methods, altering specific residues in the barnase sequence, and stop flow methods, to assess how these changes affect the rate at which the protein folds. results show that hydrophobic interactions are the main driving force in the early stages of protein folding. -- The fluid cell -- This section gives a brief snapshot of the dynamic organisation of cells, from the single-celled ameoba to mammalian cells in culture. It shows how the fluidity of cells is important not only in growth and division, but in allowing cells to communicate and make contact with each other to form tissues and organs.
Probing proteins -- This selection looks at the two main techniques for studying protein structure. With crystals as the starting point, X ray diffraction can give 3-dimensional information in atom...ic detail. For molecules in solution, nuclear magnetic resonance, or NMR, is the method of choice. What are the strengths and limitations of these techniques and in what way might they provide complementary information? One protein that has been studied in detail by both methods is the enzyme, BARNASE. This band will show the model of BARNASE that has emerged from these studies and the insights it has given about how the molecule functions. -- Molecules on the move -- The first section looks at how molecular motion in barnase has been modelled on computer graphics. what role might this dynamic behaviour play in protein function. the second section deals with another puzzle. How do proteins, built from a linear string of amino acids, fold into a 3 dimensional conformation that's both unique and biologically active? The problem of protein folding in barnase has been tackled by a combination of protein engineering methods, altering specific residues in the barnase sequence, and stop flow methods, to assess how these changes affect the rate at which the protein folds. results show that hydrophobic interactions are the main driving force in the early stages of protein folding. -- The fluid cell -- This section gives a brief snapshot of the dynamic organisation of cells, from the single-celled ameoba to mammalian cells in culture. It shows how the fluidity of cells is important not only in growth and division, but in allowing cells to communicate and make contact with each other to form tissues and organs.
| Module code and title: | S327, Living processes | |||||||||
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| Item code: | S327; VCR1 | |||||||||
| First transmission date: | 1995 | |||||||||
| Published: | 1995 | |||||||||
| Rights Statement: | ||||||||||
| Restrictions on use: | ||||||||||
| Duration: | 00:50:57 | |||||||||
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| Track listing: |
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| Producer: | Rissa de la Paz | |||||||||
| Contributors: | Jane Copland; Alan Fersht | |||||||||
| Publisher: | BBC Open University | |||||||||
| Keyword(s): | Alpha helix; Amoeba; Atomic detail; BARNASE enzyme; Cell organisation; Chromosomes; Crystals; Dynamic behaviour; Nuclear Magnetic Resonance (NMR); Protein structure; X-ray diffraction | |||||||||
| Master spool number: | DOU8051 | |||||||||
| Production number: | FOUS785K | |||||||||
| Videofinder number: | 4941 | |||||||||
| Available to public: | no | |||||||||
