Patterns in Secondary Structure Packing — a Database for Prediction
Most known structures have been derived by X-ray crystallographic means. This technique requires good quality crystals of the protein and almost all structures are of globular proteins. Because of the difficulty of crystallising membrane bound proteins, there is a paucity of structures for these (Eisenberg, 1984). 2D NMR is a relatively new technique producing distance or angle constraints which may be used to determine structures for small proteins in solution (polypeptides of up to around 100 residues have been attempted). Both methods have the practical limitation of requiring samples of the material in appropriate form and purity.
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- Abagyan, R. A. and Maiorov, V. N. (1988). A simple qualitative representation of polypeptide chain folds: Comparison of protein tertiary structures. J. Biomol. Structure & Dynamics, 5 (6): 1267–1279.Google Scholar
- Chatfield, C. and Collins, A. J. (1989). Introduction to Multivariate Analysis. Chapman and Hall.Google Scholar
- Schulz, G. E. and Schirmer, R. H. (1979). Principles of Protein Structure. Springer-Verlag.Google Scholar
- von Heijne, G. (1987). Sequence Analysis in Molecular Biology (Treasure Trove or Trivial Pursuit). Academic Press Inc.Google Scholar