Structure restraints from heteronuclear pseudocontact shifts generated by lanthanide tags at two different sites.
J Biomol NMR
; 68(1): 19-32, 2017 May.
Article
in En
| MEDLINE
| ID: mdl-28434103
Pseudocontact shifts (PCS) encode long-range information on 3D structures of protein backbones and side-chains. The level of structural detail that can be obtained increases with the number of different sites tagged with a paramagnetic metal ion to generate PCSs. Here we show that PCSs from two different sites can suffice to determine the structure of polypeptide chains and their location and orientation relative to the magnetic susceptibility tensor χ, provided that PCSs are available for 1H as well as heteronuclear spins. In addition, PCSs from two different sites are shown to provide detailed structural information on the conformation of methyl group-bearing amino-acid side-chains. A previously published ensemble structure of ubiquitin is shown to explain the magnetic susceptibility and alignment tensors slightly better than structures that try to explain the experimental data by a single conformation, illustrating the potential of PCSs as a tool to investigate small conformational changes.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Nuclear Magnetic Resonance, Biomolecular
/
Lanthanoid Series Elements
/
Ubiquitin
Language:
En
Journal:
J Biomol NMR
Journal subject:
BIOLOGIA MOLECULAR
/
DIAGNOSTICO POR IMAGEM
/
MEDICINA NUCLEAR
Year:
2017
Document type:
Article
Affiliation country:
Australia
Country of publication:
Netherlands