ReviewAdvances in experimental medicine and biology
A Hybrid Approach for Protein Structure Determination Combining Sparse NMR with Evolutionary Coupling Sequence Data.
Review in Advances in experimental medicine and biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Computational and Experimental Approaches and Applications of Biological NMR.Advances in experimental medicine and biology · 2026Review
- A computational and structural analysis of germline and somatic variants affecting the DDR mechanism, and their impact on human diseases.Scientific reports · 2021Article
- Improving integrative 3D modeling into low- to medium-resolution electron microscopy structures with evolutionary couplings.Protein science : a publication of the Protein Society · 2021Article
- Geleophysic dysplasia: novel missense variants and insights into ADAMTSL2 intracellular trafficking.Molecular genetics and metabolism reports · 2019Article
- Combining Evolutionary Covariance and NMR Data for Protein Structure Determination.Methods in enzymology · 2019Article
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Authors and funding
5 authors.
Funding
Abstract
While 3D structure determination of small (<15 kDa) proteins by solution NMR is largely automated and routine, structural analysis of larger proteins is more challenging. An emerging hybrid strategy for modeling protein structures combines sparse NMR data that can be obtained for larger proteins with sequence co-variation data, called evolutionary couplings (ECs), obtained from multiple sequence alignments of protein families. This hybrid "EC-NMR" method can be used to accurately model larger (15-60 kDa) proteins, and more rapidly determine structures of smaller (5-15 kDa) proteins using only backbone NMR data. The resulting structures have accuracies relative to reference structures comparable to those obtained with full backbone and sidechain NMR resonance assignments. The requirement that evolutionary couplings (ECs) are consistent with NMR data recorded on a specific member of a protein family, under specific conditions, potentially also allows identification of ECs that reflect alternative allosteric or excited states of the protein structure.
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