Site-specific isotopic labeling of proteins for NMR studies

1992 ◽  
Vol 114 (20) ◽  
pp. 7959-7961 ◽  
Author(s):  
Jonathan A. Ellman ◽  
Brian F. Volkman ◽  
David Mendel ◽  
Peter G. Schulz ◽  
David E. Wemmer
Keyword(s):  
Isotopic Labeling ◽  
Nmr Studies ◽  
Site Specific

Ultra-high field NMR studies of antibody binding and site-specific phosphorylation of α-synuclein

2007 ◽  
Vol 363 (3) ◽  
pp. 795-799 ◽  
Author(s):  
Hiroaki Sasakawa ◽  
Eri Sakata ◽  
Yoshiki Yamaguchi ◽  
Masami Masuda ◽  
Tetsuya Mori ◽  
...  
Keyword(s):  
High Field ◽  
Antibody Binding ◽  
Nmr Studies ◽  
Ultra High Field ◽  
Site Specific

Site-Specific d(GpG) Intrastrand Cross-Links Formed by Dinuclear Platinum Complexes. Bending and NMR Studies†

Biochemistry ◽  
1996 ◽  
Vol 35 (51) ◽  
pp. 16705-16713 ◽  
Author(s):  
J. Kašpárková ◽  
K. J. Mellish ◽  
Y. Qu ◽  
V. Brabec ◽  
N. Farrell
Keyword(s):  
Platinum Complexes ◽  
Nmr Studies ◽  
Site Specific ◽  
Dinuclear Platinum ◽  
Cross Links ◽  
Dinuclear Platinum Complexes

Dictyostelium discoideum as Expression Host: Isotopic Labeling of a Recombinant Glycoprotein for NMR Studies

2000 ◽  
Vol 19 (3) ◽  
pp. 335-342 ◽  
Author(s):  
Liza Cubeddu ◽  
Catherine X. Moss ◽  
James D. Swarbrick ◽  
Andrew A. Gooley ◽  
Keith L. Williams ◽  
...  
Keyword(s):  
Dictyostelium Discoideum ◽  
Isotopic Labeling ◽  
Nmr Studies ◽  
Recombinant Glycoprotein ◽  
Expression Host

scholarly journals Robust Cell-Free Expression of Sub-Pathological and Pathological Huntingtin Exon-1 for NMR Studies. General Approaches for the Isotopic Labeling of Low-Complexity Proteins

Biomolecules ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 1458
Author(s):  
Anna Morató ◽  
Carlos A. Elena-Real ◽  
Matija Popovic ◽  
Aurélie Fournet ◽  
Karen Zhang ◽  
...  
Keyword(s):  
Protein Expression ◽  
Expression System ◽  
Isotopic Labeling ◽  
Low Complexity ◽  
Nonsense Suppression ◽  
Sequential Assignment ◽  
Reaction Yield ◽  
Nmr Studies ◽  
Intrinsically Disordered ◽  
Exon 1

The high-resolution structural study of huntingtin exon-1 (HttEx1) has long been hampered by its intrinsic properties. In addition to being prone to aggregate, HttEx1 contains low-complexity regions (LCRs) and is intrinsically disordered, ruling out several standard structural biology approaches. Here, we use a cell-free (CF) protein expression system to robustly and rapidly synthesize (sub-) pathological HttEx1. The open nature of the CF reaction allows the application of different isotopic labeling schemes, making HttEx1 amenable for nuclear magnetic resonance studies. While uniform and selective labeling facilitate the sequential assignment of HttEx1, combining CF expression with nonsense suppression allows the site-specific incorporation of a single labeled residue, making possible the detailed investigation of the LCRs. To optimize CF suppression yields, we analyze the expression and suppression kinetics, revealing that high concentrations of loaded suppressor tRNA have a negative impact on the final reaction yield. The optimized CF protein expression and suppression system is very versatile and well suited to produce challenging proteins with LCRs in order to enable the characterization of their structure and dynamics.

Alternate-site isotopic labeling of ribonucleotides for NMR studies of ribose conformational dynamics in RNA

2006 ◽  
Vol 35 (4) ◽  
pp. 261-274 ◽  
Author(s):  
James E. Johnson ◽  
Kristine R. Julien ◽  
Charles G. Hoogstraten
Keyword(s):  
Conformational Dynamics ◽  
Isotopic Labeling ◽  
Nmr Studies
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