期刊
JOURNAL OF BIOMOLECULAR NMR
卷 41, 期 2, 页码 61-76出版社
SPRINGER
DOI: 10.1007/s10858-008-9240-8
关键词
residual dipolar couplings; alignment tensor; protein structure determination; protein GB1; ubiquitin
资金
- NIGMS NIH HHS [R01 GM075310, R01 GM075310-03, GM075310] Funding Source: Medline
The straightforward interpretation of solution state residual dipolar couplings (RDCs) in terms of internuclear vector orientations generally requires prior knowledge of the alignment tensor, which in turn is normally estimated using a structural model. We have developed a protocol which allows the requirement for prior structural knowledge to be dispensed with as long as RDC measurements can be made in three independent alignment media. This approach, called Rigid Structure from Dipolar Couplings (RSDC), allows vector orientations and alignment tensors to be determined de novo from just three independent sets of RDCs. It is shown that complications arising from the existence of multiple solutions can be overcome by careful consideration of alignment tensor magnitudes in addition to the agreement between measured and calculated RDCs. Extensive simulations as well applications to the proteins ubiquitin and Staphylococcal protein GB1 demonstrate that this method can provide robust determinations of alignment tensors and amide N-H bond orientations often with better than 10 degrees accuracy, even in the presence of modest levels of internal dynamics.
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