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Protein Engineering vol. 4 no. 2 pp. 133-135, 1990
© 1990 Oxford University Press

RESEARCH-ARTICLE

Estimating the twist of ß-strands embedded within a regular parallel ß-barrel structure

Ignace Lasters

Plant Genetic Systems Plateaustraat 22, 9000 Gent, Belgium

The parallel ß-barrel is a recurrent structural motif found in a large variety of different enzymes belonging to the family of {alpha}/ß-proteins. It has been shown previously that the hyperboloid can be considered as a scaffold describing the parallel ß-barrel structure. To assess restraints on ß-strand twist imposed by a given scaffold geometry, the notion of scaffold twist, Ts, is introduced. From Ts, the ß-strand twist (Twß) expected for a given scaffold geometry can be derived and it is verified that this computed twist can be used to identify ß-barrels characterized by good hydrogen bonding. It is noted that Twß is only slightly affected for ß-barrels differing in the number (N) of ß-strands, suggesting that restraints on main-chain conformation of ß-strands are not likely to account for the N = 8 invariability observed in natural parallel ß-barrels thereby strengthening previous work rationalizing this constancy.

Keywords: ß-barrels/de novo design/protein anatomy

Received May 15, 1990; accepted September 11, 1990.


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