Related ArticlesUse of selective Trp side chain labeling to characterize protein-protein and protein-ligand interactions by NMR spectroscopy.
J Am Chem Soc. 2003 Mar 12;125(10):2892-3
Authors: Rodriguez-Mias RA, Pellecchia M
Recent studies on amino acid occurrence in protein binding sites suggest that only a reduced number of residues are responsible for most interaction energy in protein-protein and protein-ligand interactions. Above all, tryptophan (Trp) seems to be the most frequent residue in protein's hot spots. Here we report a novel, efficient, and cost-effective method to selectively incorporate specific isotope labels into the side chains of Trp residues in recombinant proteins. We show that the method proposed allows selective NMR observation of Trp side chains that enables studies of ligand binding, protein-protein interactions, hydrogen binding, protein folding, and side chain dynamics. Examples with the protein BIR3 will be given.
Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment
Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment
Abstract Obtaining NMR assignments for slowly tumbling molecules such as detergent-solubilized membrane proteins is often compromised by low sensitivity as well as spectral overlap. Both problems can be addressed by amino-acid specific isotope labeling in conjunction with 15Nā??1H correlation experiments. In this work an extended combinatorial selective in vitro labeling scheme is proposed that seeks to reduce the number of samples required for assignment. Including three...
nmrlearner
Journal club
0
01-21-2012 06:26 PM
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Protein Pept Lett. 2011 Jan 11;
Authors: Yang D
Protein side chain dynamics is associated with protein stability, folding, and intermolecular interactions. Detailed dynamics information is crucial for the understanding of protein function and biochemical and biophysical properties, which can be obtained using NMR relaxation techniques. In this review, (13)C relaxation of methine, methylene and methyl groups with and without...
nmrlearner
Journal club
0
01-13-2011 12:00 PM
[NMR paper] NMR assignment of protein side chains using residue-correlated labeling and NOE spect
NMR assignment of protein side chains using residue-correlated labeling and NOE spectra.
Related Articles NMR assignment of protein side chains using residue-correlated labeling and NOE spectra.
J Magn Reson. 2003 Dec;165(2):237-47
Authors: Mueller GA, Kirby TW, DeRose EF, London RE
A new approach for the isotopic labeling of proteins is proposed that aims to facilitate side chain resonance assignments. Residue-correlated (RC) labeling is achieved by the expression of a protein on a medium containing a mixture of labeled, e.g., amino acids,...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studi
Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Related Articles Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Biochemistry. 2001 Jun 5;40(22):6559-69
Authors: Flynn PF, Bieber Urbauer RJ, Zhang H, Lee AL, Wand AJ
A detailed characterization of the main chain and side chain dynamics in R. capsulatus ferrocytochrome c(2) derived from (2)H NMR relaxation of methyl group resonances is...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NM
Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative ferredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative ferredoxin.
Arch Biochem Biophys. 1995 Jan 10;316(1):619-34
Authors: Cheng H, Westler WM, Xia B, Oh BH, Markley JL
Two alternative T7 RNA promoter/polymerase systems...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] URPI: a utility program for planning selective protein double-labeling with 13C and 1
URPI: a utility program for planning selective protein double-labeling with 13C and 15N in NMR analyses.
Related Articles URPI: a utility program for planning selective protein double-labeling with 13C and 15N in NMR analyses.
J Magn Reson B. 1994 Jan;103(1):89-90
Authors: Shinagawa K, Ohya M, Wakamatsu K
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] URPI: a utility program for planning selective protein double-labeling with 13C and 1
URPI: a utility program for planning selective protein double-labeling with 13C and 15N in NMR analyses.
Related Articles URPI: a utility program for planning selective protein double-labeling with 13C and 15N in NMR analyses.
J Magn Reson B. 1994 Jan;103(1):89-90
Authors: Shinagawa K, Ohya M, Wakamatsu K
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] Selective and extensive 13C labeling of a membrane protein for solid-state NMR invest
Selective and extensive 13C labeling of a membrane protein for solid-state NMR investigations.
Related Articles Selective and extensive 13C labeling of a membrane protein for solid-state NMR investigations.
J Biomol NMR. 1999 May;14(1):71-4
Authors: Hong M, Jakes K
The selective and extensive 13C labeling of mostly hydrophobic amino acid residues in a 25 kDa membrane protein, the colicin Ia channel domain, is reported. The novel 13C labeling approach takes advantage of the amino acid biosynthetic pathways in bacteria and suppresses the...
Use of selective Trp side chain labeling to characterize protein-protein and protein-
Linear Mode
