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A survey of left-handed polyproline II helices

โœ Scribed by Benjamin J. Stapley; Trevor P. Creamer

Book ID
111753592
Publisher
Cold Spring Harbor Laboratory Press
Year
2008
Tongue
English
Weight
268 KB
Volume
8
Category
Article
ISSN
0961-8368

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The left-handed polyproline II helix (PPII) is believed to be the preferred conformation for proline-rich regions of sequence in proteins. Such regions have been postulated to be protein-protein interaction domains. The formation of this structure is studied here using simple Monte Carlo computer si

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Spherulites of poly-L-proline I1 were grown by film casting from a dilute formic acid solution. Electron diffraction indicated that the molecular axis was parallel to the surface and essentially normal to the face of the lamellae. The molecular length was five times greater than the width of the lam