A DOTA-amide lanthanide tag for reliable generation of pseudocontact shifts in protein NMR spectra.
A DOTA-amide lanthanide tag for reliable generation of pseudocontact shifts in protein NMR spectra.
A DOTA-amide lanthanide tag for reliable generation of pseudocontact shifts in protein NMR spectra.
Bioconjug Chem. 2011 Aug 31;
Authors: Graham B, Loh CT, Swarbrick JD, Ung P, Shin J, Yagi H, Jia X, Chhabra S, Barlow N, Pintacuda G, Huber T, Otting G
Abstract
Structural studies of proteins and protein-ligand complexes by nuclear magnetic resonance (NMR) spectroscopy can be greatly enhanced by site-specific attachment of lanthanide ions to...
nmrlearner
Journal club
0
09-01-2011 05:20 PM
Proteinā??protein HADDocking using exclusively pseudocontact shifts
Proteinā??protein HADDocking using exclusively pseudocontact shifts
<div class="Abstract" lang="en">Abstract <div class="normal">In order to enhance the structure determination process of macromolecular assemblies by NMR, we have implemented long-range pseudocontact shift (PCS) restraints into the data-driven protein docking package HADDOCK. We demonstrate the efficiency of the method on a synthetic, yet realistic case based on the lanthanide-labeled N-terminal Īµ domain of the E. coli DNA polymerase III (Īµ186) in complex with the HOT domain. Docking from the bound form of the two...
nmrlearner
Journal club
0
06-06-2011 12:53 AM
Generation of Pseudocontact Shifts in Protein NMR Spectra with a Genetically Encoded
Generation of Pseudocontact Shifts in Protein NMR Spectra with a Genetically Encoded Cobalt(II)-Binding Amino Acid.
Related Articles Generation of Pseudocontact Shifts in Protein NMR Spectra with a Genetically Encoded Cobalt(II)-Binding Amino Acid.
Angew Chem Int Ed Engl. 2010 Nov 25;
Authors: Nguyen TH, Ozawa K, Stanton-Cook M, Barrow R, Huber T, Otting G
nmrlearner
Journal club
0
11-27-2010 02:45 PM
[NMR paper] Improving the accuracy of NMR structures of large proteins using pseudocontact shifts
Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints.
Related Articles Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints.
J Biomol NMR. 2004 Mar;28(3):205-12
Authors: Gaponenko V, Sarma SP, Altieri AS, Horita DA, Li J, Byrd RA
We demonstrate improved accuracy in protein structure determination for large (>/=30 kDa), deuterated proteins (e.g. STAT4(NT)) via the combination of pseudocontact shifts for amide and methyl protons...
nmrlearner
Journal club
0
11-24-2010 09:25 PM
[NMR paper] Exploring the DNA binding domain of gene V protein encoded by bacteriophage M13 with
Exploring the DNA binding domain of gene V protein encoded by bacteriophage M13 with the aid of spin-labeled oligonucleotides in combination with 1H-NMR.
Related Articles Exploring the DNA binding domain of gene V protein encoded by bacteriophage M13 with the aid of spin-labeled oligonucleotides in combination with 1H-NMR.
Biochemistry. 1993 Sep 14;32(36):9407-16
Authors: Folkers PJ, van Duynhoven JP, van Lieshout HT, Harmsen BJ, van Boom JH, Tesser GI, Konings RN, Hilbers CW
The DNA binding domain of the single-stranded DNA binding protein...
nmrlearner
Journal club
0
08-22-2010 03:01 AM
[NMR paper] Determinants of protein hyperthermostability: purification and amino acid sequence of
Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR.
Related Articles Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR.
Biochemistry. 1991 Nov 12;30(45):10885-95
Authors: Blake PR, Park JB, Bryant FO, Aono S, Magnuson JK, Eccleston E, Howard...
nmrlearner
Journal club
0
08-21-2010 11:12 PM
[NMR paper] Determinants of protein hyperthermostability: purification and amino acid sequence of
Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR.
Related Articles Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR.
Biochemistry. 1991 Nov 12;30(45):10885-95
Authors: Blake PR, Park JB, Bryant FO, Aono S, Magnuson JK, Eccleston E, Howard...
nmrlearner
Journal club
0
08-21-2010 11:12 PM
Numbat: an interactive software tool for fitting Δχ-tensors to molecular coordinates using pseudocontact shifts
Numbat: an interactive software tool for fitting Δχ-tensors to molecular coordinates using pseudocontact shifts
Christophe Schmitz, Mitchell J. Stanton-Cook, Xun-Cheng Su, Gottfried Otting and Thomas Huber
Journal of Biomolecular NMR; 2008; 41(3) pp 179 - 189
Abstract:
Pseudocontact shift (PCS) effects induced by a paramagnetic lanthanide bound to a protein have become increasingly popular in NMR spectroscopy as they yield a complementary set of orientational and long-range structural restraints. PCS are a manifestation of the χ-tensor anisotropy, the Δχ-tensor, which in turn can be...