Efficient segmental isotope labeling of multi-domain proteins using Sortase A View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2015-09

AUTHORS

Lee Freiburger, Miriam Sonntag, Janosch Hennig, Jian Li, Peijian Zou, Michael Sattler

ABSTRACT

NMR studies of multi-domain protein complexes provide unique insight into their molecular interactions and dynamics in solution. For large proteins domain-selective isotope labeling is desired to reduce signal overlap, but available methods require extensive optimization and often give poor ligation yields. We present an optimized strategy for segmental labeling of multi-domain proteins using the S. aureus transpeptidase Sortase A. Critical improvements compared to existing protocols are (1) the efficient removal of cleaved peptide fragments by centrifugal filtration and (2) a strategic design of cleavable and non-cleavable affinity tags for purification. Our approach enables routine production of milligram amounts of purified segmentally labeled protein for NMR and other biophysical studies. More... »

PAGES

1-8

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10858-015-9981-0

DOI

http://dx.doi.org/10.1007/s10858-015-9981-0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1004886800

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26319988


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