An analysis of the amino acid distributions at 15 positions, viz., NЉ, NЈ, Ncap, N1, N2, N3, N4, Mid, C4, C3, C2, C1, Ccap, CЈ, and CЉ in 1,131 ␣-helices reveals that each position has its own unique characteristics. In general, natural helix sequences optimize by identifying the residues to be avoi
Helical segment analysis of α-helical regions in proteins
✍ Scribed by S. S. Rajan; R. Srinivasan
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1977
- Tongue
- English
- Weight
- 746 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The methods suggested earlier for the analysis and representation of protein structural data are now extended to the helical regions in finer details. These enable better handling of characterization of bends and distortions, for which statistical parameters are also developed. Using latest myoglobin data, best experimental parameters for the α‐helix are deduced to be r~N~ = 1.55 (0.13) Å, r = 2.28 (0.12) Å, r~C′~ = 1.70 (0.10) Å, r~0~ = 2.02 (0.12) Å, ϕ = 100.5 (2.3)°, and t = 1.495 (0.055) Å.
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