[NMR paper] Assessment of Prediction Methods for Protein Structures Determined by NMR in CASP14: Impact of AlphaFold2
Assessment of Prediction Methods for Protein Structures Determined by NMR in CASP14: Impact of AlphaFold2
NMR studies can provide unique information about protein conformations in solution. In CASP14, three reference structures provided by solution NMR methods were available (T1027, T1029, and T1055), as well as a fourth data set of NMR-derived contacts for an integral membrane protein (T1088). For the three targets with NMR-based structures, the best prediction results ranged from very good (GDT_TS = 0.90, for T1055) to poor (GDT_TS = 0.47, for T1029). We explored the basis of these...
Assessment of prediction methods for protein structures determined by NMR in CASP14: Impact of AlphaFold2 - Wiley Online Library
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