Determination of solution structures of paramagnetic proteins by NMR

Standard procedures for using nuclear Overhauser enhancements (NOE) between protons to generate structures for diamagnetic proteins in solution from NMR data may be supplemented by using dipolar shifts if the protein is paramagnetic. This is advantageous since the electron -nuclear dipolar coupling...

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Bibliographic Details
Published in:European biophysics journal 1998-01, Vol.27 (4), p.367-375
Main Authors: Turner, D L, Brennan, L, Chamberlin, S G, Louro, R O, Xavier, A V
Format: Article
Language:English
Subjects:
Anisotropy
Biophysical Phenomena
Biophysics
Heme - chemistry
Magnetic properties
Magnetic Resonance Spectroscopy
Magnetics
Models, Chemical
Models, Molecular
NMR
Nuclear magnetic resonance
Peroxidases - chemistry
Proteins
Proteins - chemistry
Software
Solutions
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Summary:Standard procedures for using nuclear Overhauser enhancements (NOE) between protons to generate structures for diamagnetic proteins in solution from NMR data may be supplemented by using dipolar shifts if the protein is paramagnetic. This is advantageous since the electron -nuclear dipolar coupling provides relatively long-range geometric information with respect to the paramagnetic centre which complements the short-range distance constraints NOEs. Several different strategies have been developed to date, but none of these attempts to combine data from NOEs and dipolar shifts in the initial stages of structure calculation or to determine three dimensional protein structures together with their magnetic properties. This work shows that the magnetic and atomic structures are highly correlated and that it is important to have additional constraints both to provide starting parameters for the magnetic properties and to improve the definition of the best fit. Useful parameters can be obtained for haem proteins from Fermi contact shifts; this approach is compared with a new method based on the analysis of dipolar shifts in haem methyl groups with respect to data from horse and tuna ferricytochromes c. The methods developed for using data from NOEs and dipolar shifts have been incorporated in a new computer program, PARADYANA, which is demonstrated in application to a model data set for the sequence of the haem octapeptide known as microperoxidase-8.
ISSN:0175-7571
1432-1017
DOI:10.1007/s002490050144