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Assignment of protein backbone resonances using connectivity, torsion angles and13Cαchemical shifts

✍ Scribed by Laura C. Morris; Homayoun Valafar; James H. Prestegard

Book ID
111591416
Publisher
Springer Netherlands
Year
2004
Tongue
English
Weight
220 KB
Volume
29
Category
Article
ISSN
0925-2738

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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