Related ArticlesEvaluation of protein adsorption and preferred binding regions in multimodal chromatography using NMR.
Proc Natl Acad Sci U S A. 2010 Sep 13;
Authors: Chung WK, Freed AS, Holstein MA, McCallum SA, Cramer SM
NMR titration experiments with labeled human ubiquitin were employed in concert with chromatographic data obtained with a library of ubiquitin mutants to study the nature of protein adsorption in multimodal (MM) chromatography. The elution order of the mutants on the MM resin was significantly different from that obtained by ion-exchange chromatography. Further, the chromatographic results with the protein library indicated that mutations in a defined region induced greater changes in protein affinity to the solid support. Chemical shift mapping and determination of dissociation constants from NMR titration experiments with the MM ligand and isotopically enriched ubiquitin were used to determine and rank the relative binding affinities of interaction sites on the protein surface. The results with NMR confirmed that the protein possessed a distinct preferred binding region for the MM ligand in agreement with the chromatographic results. Finally, coarse-grained ligand docking simulations were employed to study the modes of interaction between the MM ligand and ubiquitin. The use of NMR titration experiments in concert with chromatographic data obtained with protein libraries represents a previously undescribed approach for elucidating the structural basis of protein binding affinity in MM chromatographic systems.
PMID: 20837551 [PubMed - as supplied by publisher]
[NMR paper] Mapping the interacting regions between troponins T and C. Binding of TnT and TnI pep
Mapping the interacting regions between troponins T and C. Binding of TnT and TnI peptides to TnC and NMR mapping of the TnT-binding site on TnC.
Related Articles Mapping the interacting regions between troponins T and C. Binding of TnT and TnI peptides to TnC and NMR mapping of the TnT-binding site on TnC.
J Biol Chem. 2001 Sep 28;276(39):36606-12
Authors: Blumenschein TM, Tripet BP, Hodges RS, Sykes BD
Muscular contraction is triggered by an increase in calcium concentration, which is transmitted to the contractile proteins by the troponin...
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Evaluation of protein adsorption and preferred binding regions in multimodal chromato
Evaluation of protein adsorption and preferred binding regions in multimodal chromatography using NMR
Chung, W. K., Freed, A. S., Holstein, M. A., McCallum, S. A., Cramer, S. M....
Date: 2010-09-28
NMR titration experiments with labeled human ubiquitin were employed in concert with chromatographic data obtained with a library of ubiquitin mutants to study the nature of protein adsorption in multimodal (MM) chromatography. The elution order of the mutants on the MM resin was significantly different from that obtained by ion-exchange chromatography. Further, the chromatographic results...
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09-28-2010 10:03 PM
Crystallographic and NMR evaluation of the impact of peptide binding to the second PD
Crystallographic and NMR evaluation of the impact of peptide binding to the second PDZ domain of PTP1E.
Crystallographic and NMR evaluation of the impact of peptide binding to the second PDZ domain of PTP1E.
Biochemistry. 2010 Sep 14;
Authors: Zhang J, Sapienza PJ, Ke H, Chang A, Hengel SR, Wang H, Phillips GN, Lee AL
PDZ (PSD95/Discs large/ZO-1) domains are ubiquitous protein interaction motifs found in scaffolding proteins involved in signal transduction. Despite the fact that many PDZs show a limited tendency to undergo structural change, the...
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09-16-2010 02:59 PM
[NMR paper] Evaluation of Solvent Accessibility to the [Fe(4)S(4)] Binding Pocket in Native and T
Evaluation of Solvent Accessibility to the Binding Pocket in Native and Tyr19 Mutant High Potential Iron Proteins by (1)H-(15)N HMQC and (19)F NMR Experiments.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Evaluation of Solvent Accessibility to the Binding Pocket in Native and Tyr19 Mutant High Potential Iron Proteins by (1)H-(15)N HMQC and (19)F NMR Experiments.
Inorg Chem. 1996 Feb 28;35(5):1121-1125
Authors: Li D, Agarwal A, Cowan JA
The solvent accessibility of Chromatium...
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[NMR paper] NMR studies of peptides derived from the putative binding regions of cartilage protei
NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
Related Articles NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
J Biol Chem. 1994 Jan 21;269(3):1699-704
Authors: Horita DA, Hajduk PJ, Goetinck PF, Lerner LE
Previous work has implicated sequences within the tandem repeats of cartilage link protein in the interaction of link protein with hyaluronan. This conclusion was based on...
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08-22-2010 03:33 AM
[NMR paper] NMR evidence for similarities between the DNA-binding regions of Drosophila melanogas
NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors.
Related Articles NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors.
Biochemistry. 1994 Jan 11;33(1):10-6
Authors: Vuister GW, Kim SJ, Wu C, Bax A
Heteronuclear multidimensional NMR experiments of residues 33-163 of the...
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08-22-2010 03:33 AM
[NMR paper] NMR studies of peptides derived from the putative binding regions of cartilage protei
NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
Related Articles NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
J Biol Chem. 1994 Jan 21;269(3):1699-704
Authors: Horita DA, Hajduk PJ, Goetinck PF, Lerner LE
Previous work has implicated sequences within the tandem repeats of cartilage link protein in the interaction of link protein with hyaluronan. This conclusion was based on...
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Journal club
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08-22-2010 03:33 AM
[NMR paper] NMR evidence for similarities between the DNA-binding regions of Drosophila melanogas
NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors.
Related Articles NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors.
Biochemistry. 1994 Jan 11;33(1):10-6
Authors: Vuister GW, Kim SJ, Wu C, Bax A
Heteronuclear multidimensional NMR experiments of residues 33-163 of the...