Biomedical Engineering Reference
In-Depth Information
symmetry and a backbone RMSD 1.1
˚
from the crystal structure. By
comparison, models calculated using C
4
symmetry failed to converge and
possessed much higher average energies. It therefore seems that
ROSETTAOligomers has potential to distinguish between different point
groups solely from sparse NMR data.
176
3.10 Conclusions
Protein
1
H,
13
C and
15
N chemical shifts can be measured easily to high
accuracy and act as richly detailed probes of protein structure and dynamics.
Recently developed computational procedures that take chemical shift and
primary sequence data as input can classify secondary structure, define specific
torsion angles, and even determine atomic-resolution models of isolated
domains, homo-oligomeric systems and protein-protein complexes. This
powerful use of sparse NMR data is already finding wide applications in
structural genomics pipelines and promises to provide new structural insights
into species that are difficult to study by other means, such as sparsely
populated excited states and transiently formed intermediates.
Acknowledgements
Rob Beagrie, Nicole Cheung, Mahon Maguire, Ricardo Montavao, Paul
Robustelli and Tim Stevens are thanked for illuminating conversations.
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