Thermodynamics of left-handed helix formation
β Scribed by H.H. Klump
- Book ID
- 115917865
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 519 KB
- Volume
- 196
- Category
- Article
- ISSN
- 0014-5793
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π SIMILAR VOLUMES
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
A conformational study of poly-L-serine has shown that it can exist in the left-handed Ξ±-helical form. A study of a pair of peptide units with the serine sidegroup attached to the Ξ± carbon atom linking the two units showed that Oο£ΏH βO hydrogen bonds between the OH group of the side chain and a carbo