Literature DB >> 27295425

Isotope-labeling strategies for solution NMR studies of macromolecular assemblies.

Heyi Zhang1, Hugo van Ingen2.   

Abstract

Proteins come together in macromolecular assemblies, recognizing and binding to each other through their structures, and operating on their substrates through their motions. Detailed characterization of these processes is particularly suited to NMR, a high-resolution technique sensitive to structure, dynamics, and interactions. Advances in isotope-labeling have enabled such studies to an ever-increasing range of systems. Here we highlight recent applications and bring to the fore the range of options to produce labeled proteins and to control the specific placement of isotopes. The increased labeling control and affordability, together with the possibility to combine strategies will further deepen and extend the range of protein assembly investigations.
Copyright © 2016. Published by Elsevier Ltd.

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Year:  2016        PMID: 27295425     DOI: 10.1016/j.sbi.2016.05.008

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  10 in total

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7.  Methyl group assignment using pseudocontact shifts with PARAssign.

Authors:  Mathilde Lescanne; Simon P Skinner; Anneloes Blok; Monika Timmer; Linda Cerofolini; Marco Fragai; Claudio Luchinat; Marcellus Ubbink
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Authors:  Alistair M Jagger; Christopher A Waudby; James A Irving; John Christodoulou; David A Lomas
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9.  Anthranilic acid, the new player in the ensemble of aromatic residue labeling precursor compounds.

Authors:  Julia Schörghuber; Leonhard Geist; Marilena Bisaccia; Frederik Weber; Robert Konrat; Roman J Lichtenecker
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10.  Automatic structure-based NMR methyl resonance assignment in large proteins.

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  10 in total

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