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Collapse of a polypeptide chain as a result of the intramolecular formation of antiparallel β-sheets

✍ Scribed by Luanne F. Tilstra; Wayne L. Mattice

Publisher
Wiley (John Wiley & Sons)
Year
1988
Tongue
English
Volume
27
Category
Article
ISSN
0006-3525

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✦ Synopsis

The folded nature of an intramolecular antiparallel 8-sheet suggests that the introduction of this structure into a statistical coil might be accompanied by a contraction of the chain. The magnitude of the contraction, and the conditions that produce the maximum contraction, have been assessed by the combination of generator matrices with an earlier formulation for the configuration partition function. The results show that the mean square dimensions do indeed pass through a minimum upon the transition from a statistical coil to an antiparallel 8-sheet. The depth of the minimum is relatively insensitive to the values of I3 and T , provided the assignments are within the physically sensible range. (The borders of the ordered region are assumed to be of higher energy than the interior.) In contrast with the depth of the minimum, the P-sheet content that produces the minimum is quite sensitive to plausible variation in I3 and T. A much greater collapse of the chain can be produced by antiparallel 8-sheet formation than that found in the course of the helix-coil transition. The collapse may cause the volume pervaded by the chain to come within an order of magnitude of the volume characteristic of the globular state.

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