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Relation between structure and function of α/β–protejns*

Published online by Cambridge University Press:  17 March 2009

Carl-Ivar Brändén
Carl-Ivar Brändén
Affiliation:
Department of Chemistry and Molecular Biology, SwedishUniversity of Agricultural Sciences, 750 07 Uppsala
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Extract

Protein chains are usually folded into one or several discrete globular units called domains (Schulz & Schirmer, 1979). Levitt & Chothia (1976) have shown that the structures of such domains frequently fall into one of the following three classes; α-proteins which are mainly α-helical, β-proteins which contain antiparallel β-strands and α/β proteins which have a central core consisting of a sheet of strands, most of which are parallel. The connexions between the parallel strands in αβ-proteins frequently contain helices which are packed on both sides of the sheet in a regular way (Chothia, Levitt & Richardson, 1977).

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Research Article
Information
Quarterly Reviews of Biophysics , Volume 13 , Issue 3 , August 1980 , pp. 317 - 338
Copyright
Copyright © Cambridge University Press 1980

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References

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