Relation between Functional Loop Regions and Intron Positions in α/ß Domains

  • Carl-Ivar Bränden
Part of the NATO ASI Series book series (NSSA, volume 126)


It is generally recognised that protein molecules are arrangend into small folding units domains. We now have a sufficiently large sample of three dimensional structures to realise that there is only a limited number of different folding patterns for such domains (Richardson, 1981). The most common type of these patterns are the α/ß domains which comprise around 25% of all known domain structures. The central fold of these domains is \/ery simple consisting of a number of hydrogen bonded parallel strands joined by helices. The strands all have their NH2 ends at the same edge of the resulting ß-sheet. The sheet thus has a polarity with an NH2-edge and a C00H edge. Loop regions, which are usually relatively short, join the strands to the helices at both ends.


Active Site Residue Triosephosphate Isomerase Intron Position Functional Residue Glyceraldehyde Phosphate 
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Copyright information

© Springer Science+Business Media New York 1987

Authors and Affiliations

  • Carl-Ivar Bränden
    • 1
  1. 1.Department of Molecular BiologySwedish University of Agricultural Sciences, Uppsala Biomedical CenterUppsalaSweden

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