Refinement of protein structure against non-redundant carbonyl 13C NMR relaxation.

Refinement of protein structure against non-redundant carbonyl 13C NMR relaxation.
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针对非冗余羰基 13C NMR 弛豫精修蛋白质结构。

DOI:
10.1007/s10858-007-9165-7
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发表时间:
2007
影响因子:
2.7
通讯作者:
Chang,Shou-Lin
Chang,Shou-Lin
中科院分区:
生物学3区
文献类型:
--
作者:
Tjandra,Nico;Suzuki,Motoshi;Chang,Shou-Lin

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Carbonyl13C′ relaxation is dominated by the contribution from the13C′ chemical shift anisotropy (CSA). The relaxation rates provide useful and non-redundant structural information in addition to dynamic parameters. It is straightforward to acquire, and offers complimentary structural information to the15N relaxation data. Furthermore, the non-axial nature of the13C′ CSA tensor results in a T1/T2value that depends on an additional angular variable even when the diffusion tensor of the protein molecule is axially symmetric. This dependence on an extra degree of freedom provides new geometrical information that is not available from the NH dipolar relaxation. A protocol that incorporates such structural restraints into NMR structure calculation was developed within the program Xplor-NIH. Its application was illustrated with the yeast Fis1 NMR structure. Refinement against the13C′ T1/T2improved the overall quality of the structure, as evaluated by cross-validation against the residual dipolar coupling as well as the15N relaxation data. In addition, possible variations of the CSA tensor were addressed.
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DOI: 10.1056/nejm197311152892008
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