1j4v
From Proteopedia
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==Overview== | ==Overview== | ||
| - | A simple and robust method for determining the relative orientations of | + | A simple and robust method for determining the relative orientations of covalently linked protein domains using conjoined rigid body/torsion angle dynamics simulated annealing on the basis of residual dipolar couplings is presented. In this approach each domain is treated as a rigid body and the relevant degrees of conformational freedom are restricted to the backbone torsion angles (phi, psi) of the linker between the domains. By this means translational information afforded by the presence of an intact linker is preserved. We illustrate this approach using the domain-swapped dimer of the HIV-inactivating protein cyanovirin-N as an example. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Nostoc ellipsosporum]] | [[Category: Nostoc ellipsosporum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bewley, C | + | [[Category: Bewley, C A.]] |
| - | [[Category: Clore, G | + | [[Category: Clore, G M.]] |
[[Category: cyanovirin-n]] | [[Category: cyanovirin-n]] | ||
[[Category: dipolar couplings / conjoined rigid body-torsion angle dynamics]] | [[Category: dipolar couplings / conjoined rigid body-torsion angle dynamics]] | ||
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[[Category: nmr]] | [[Category: nmr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:00 2008'' |
Revision as of 11:19, 21 February 2008
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CYANOVIRIN-N
Overview
A simple and robust method for determining the relative orientations of covalently linked protein domains using conjoined rigid body/torsion angle dynamics simulated annealing on the basis of residual dipolar couplings is presented. In this approach each domain is treated as a rigid body and the relevant degrees of conformational freedom are restricted to the backbone torsion angles (phi, psi) of the linker between the domains. By this means translational information afforded by the presence of an intact linker is preserved. We illustrate this approach using the domain-swapped dimer of the HIV-inactivating protein cyanovirin-N as an example.
About this Structure
1J4V is a Single protein structure of sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA.
Reference
Using conjoined rigid body/torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings., Clore GM, Bewley CA, J Magn Reson. 2002 Feb;154(2):329-35. PMID:11846592
Page seeded by OCA on Thu Feb 21 13:19:00 2008
