Torsion angle restraints are frequently used in the determination and refinement of protein structures by NMR. These restraints may be obtained by J coupling, cross-correlation measurements, nuclear Overhauser effects (NOEs) or secondary chemical shifts. Currently most backbone (phi/psi) torsion ang
β¦ LIBER β¦
The prediction of protein structural class using averaged chemical shifts
β Scribed by Lin, Hao; Ding, Chen; Song, Qiang; Yang, Ping; Ding, Hui; Deng, Ke-Jun; Chen, Wei
- Book ID
- 126770659
- Publisher
- Adenine Press
- Year
- 2012
- Tongue
- English
- Weight
- 145 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0739-1102
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## Abstract Knowledge of structural classes is useful in understanding of folding patterns in proteins. Although existing structural class prediction methods applied virtually all stateβofβtheβart classifiers, many of them use a relatively simple protein sequence representation that often includes
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