On the use of residual dipolar couplings in multi-state structure calculation of two-domain proteins

Residual dipolar couplings (RDCs) are powerful nuclear magnetic resonance (NMR) probes for the structure calculation of biomacromolecules. Typically, an alignment tensor that defines the orientation of the entire molecule relative to the magnetic field is determined either before refinement of indiv...

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Vydáno v:Magnetic resonance letters Ročník 2; číslo 2; s. 61 - 68
Hlavní autoři: Born, Alexandra, Henen, Morkos A., Nichols, Parker J., Vögeli, Beat
Médium: Journal Article
Jazyk:angličtina
Vydáno: Elsevier B.V 01.05.2022
KeAi Communications Co. Ltd
Témata:
Multi-state structure
RDC
Residual dipolar coupling
Two-domain protein
RDC
Residual dipolar coupling
Two-domain protein
Multi-state structure
ISSN:2772-5162, 2097-0048, 2772-5162
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Shrnutí:Residual dipolar couplings (RDCs) are powerful nuclear magnetic resonance (NMR) probes for the structure calculation of biomacromolecules. Typically, an alignment tensor that defines the orientation of the entire molecule relative to the magnetic field is determined either before refinement of individual bond vectors or simultaneously with this refinement. For single-domain proteins this approach works well since all bond vectors can be described within the same coordinate frame, which is given by the alignment tensor. However, novel approaches are sought after for systems where no universal alignment tensor can be used. Here, we present an approach that can be applied to two-domain proteins that enables the calculation of multiple states within each domain as well as with respect to the relative positions of the two domains. The use of residual dipolar couplings in multi-state structure calculation with two-domain proteins is challenge. Here we present a protocol that relies on a two-step calculation using alignment tensors of both domains. [Display omitted]
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ISSN:2772-5162
2097-0048
2772-5162
DOI:10.1016/j.mrl.2021.10.003