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
The ESR determination of protein α-helicity
✍ Scribed by K. M. Lvov; Yu. A. Kim
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1975
- Tongue
- English
- Weight
- 467 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Experimental data are summarized on decay kinetics of uv‐induced paramagnetic centers in globular proteins. The PC decay rate in the absence of oxygen in α helical regions is shown to differ always by about two orders from that in nonhelical regions of the polypeptide chain. This effect can be utilized to estimate the degree of α helicity in the dry state, in solution, and in the frozen solution of proteins.
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