Dipoles of the α-helix and β-sheet: their role in protein folding
✍ Scribed by Hol, Wim G. J.; Halie, Louis M.; Sander, Christian
- Book ID
- 109724986
- Publisher
- Nature Publishing Group
- Year
- 1981
- Tongue
- English
- Weight
- 539 KB
- Volume
- 294
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/294532a0
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📜 SIMILAR VOLUMES
Folding type-specific secondary structure propensities of 20 naturally occurring amino acids have been derived from a-helical, b-sheet, a/b, and a/b proteins of known structures. These data show that each residue type of amino acids has intrinsic propensities in different regions of secondary struct
To determine when secondary structure forms as two chains coalesce to form an alpha-helical dimer, the folding rates of variants of the coiled coil region of GCN4 were compared. Residues at non-perturbing positions along the exterior length of the helices were substituted one at a time with alanine
## Abstract Classical descriptions of the three‐dimensional shapes of proteins usually invoke three main structures: α‐helix, β‐sheet, and β‐turn. More recently, the polyproline II (PPII) structure has been implicated in diverse biological activities including signal transduction, transcription, ce