Related ArticlesA Non-Invasive NMR Method Based on Histidine Imidazoles to Analyze the pH-Modulation of Protein-Nucleic Acid Interfaces.
Chemistry. 2015 Apr 1;
Authors: Cruz-Gallardo I, Del Conte R, Velázquez-Campoy A, García-Mauriño SM, Díaz-Moreno I
Abstract
A useful (2) J(N?H) coupling-based NMR spectroscopic approach is proposed to unveil, at the molecular level, the contribution of the imidazole groups of histidines from RNA/DNA-binding proteins on the modulation of binding to nucleic acids by pH. Such protonation/deprotonation events have been monitored on the single His96 located at the second RNA/DNA recognition motif (RRM2) of T-cell intracellular antigen-1 (TIA-1) protein. The pKa values of the His96 ionizable groups were substantially higher in the complexes with short U-rich RNA and T-rich DNA oligonucleotides than those of the isolated TIA-1 RRM2. Herein, the methodology applied to determine changes in pKa of histidine side chains upon DNA/RNA binding, gives valuable information to understand the pH effect on multidomain DNA/RNA-binding proteins that shuttle among different cellular compartments.
PMID: 25846236 [PubMed - as supplied by publisher]
[NMR paper] NMR studies on protein-nucleic acid interaction.
NMR studies on protein-nucleic acid interaction.
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J Biomol NMR. 2013 May 9;
Authors: Kaptein R
Abstract
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[NMR images] Nucleic acid and protein NMR
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11-12-2011 01:40 AM
The NMR restraints grid at BMRB for 5,266 protein and nucleic acid PDB entries
The NMR restraints grid at BMRB for 5,266 protein and nucleic acid PDB entries
Abstract Several pilot experiments have indicated that improvements in older NMR structures can be expected by applying modern software and new protocols (Nabuurs et al. in Proteins 55:483â??186, 2004; Nederveen et al. in Proteins 59:662â??672, 2005; Saccenti and Rosato in J Biomol NMR 40:251â??261, 2008). A recent large scale X-ray study also has shown that modern software can significantly improve the quality of X-ray structures that were deposited more than a few years ago (Joosten et al. in J. Appl...
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[NMR paper] An NMR method for the determination of protein-binding interfaces using dioxygen-indu
An NMR method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement.
Related Articles An NMR method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement.
J Am Chem Soc. 2005 Apr 27;127(16):5826-32
Authors: Sakakura M, Noba S, Luchette PA, Shimada I, Prosser RS
Using oxygen as a paramagnetic probe, researchers can routinely study topologies and protein-binding interfaces by NMR. The paramagnetic contribution to the amide (1)H...
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[NMR paper] NMR studies of protein-nucleic acid interactions.
NMR studies of protein-nucleic acid interactions.
Related Articles NMR studies of protein-nucleic acid interactions.
Methods Mol Biol. 2004;278:289-312
Authors: Varani G, Chen Y, Leeper TC
Protein-DNA and protein-RNA complexes play key functional roles in every living organism. Therefore, the elucidation of their structure and dynamics is an important goal of structural and molecular biology. Nuclear magnetic resonance (NMR) studies of protein and nucleic acid complexes have common features with studies of protein-protein complexes: the...
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[NMR paper] A novel NMR method for determining the interfaces of large protein-protein complexes.
A novel NMR method for determining the interfaces of large protein-protein complexes.
Related Articles A novel NMR method for determining the interfaces of large protein-protein complexes.
Nat Struct Biol. 2000 Mar;7(3):220-3
Authors: Takahashi H, Nakanishi T, Kami K, Arata Y, Shimada I
Identification of the interfaces of large (Mr > 50,000) protein-protein complexes in solution by high resolution NMR has typically been achieved using experiments involving chemical shift perturbation and/or hydrogen-deuterium exchange of the main chain amide...
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[NMR paper] Use of 1H NMR spectroscopy and computer simulations To analyze histidine pKa changes
Use of 1H NMR spectroscopy and computer simulations To analyze histidine pKa changes in a protein tyrosine phosphatase: experimental and theoretical determination of electrostatic properties in a small protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Use of 1H NMR spectroscopy and computer simulations To analyze histidine pKa changes in a protein tyrosine phosphatase: experimental and theoretical determination of electrostatic properties in a small protein.
Biochemistry. 1997 Sep 30;36(39):11984-94
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[NMR paper] NMR - this other method for protein and nucleic acid structure determination.
NMR - this other method for protein and nucleic acid structure determination.
Related Articles NMR - this other method for protein and nucleic acid structure determination.
Acta Crystallogr D Biol Crystallogr. 1995 May 1;51(Pt 3):249-70
Authors: Wüthrich K
For a quarter of a century X-ray diffraction in single crystals was unique in its ability to solve three-dimensional structures of proteins and nucleic acids at atomic resolution. The situation changed in 1984 with the completion of a protein structure determination by nuclear magnetic...
A Non-Invasive NMR Method Based on Histidine Imidazoles to Analyze the pH-Modulation of Protein-Nucleic Acid Interfaces.
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