Modular protein-RNA interactions regulating mRNA metabolism: a role for NMR.
Modular protein-RNA interactions regulating mRNA metabolism: a role for NMR.
Modular protein-RNA interactions regulating mRNA metabolism: a role for NMR.
Eur Biophys J. 2011 Apr 7;
Authors: Cukier CD, Ramos A
Here we review the role played by transient interactions between multi-functional proteins and their RNA targets in the regulation of mRNA metabolism, and we describe the important function of NMR spectroscopy in the study of these systems. We place emphasis on a general approach for the study of different features of modular multi-domain...
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04-08-2011 10:00 AM
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
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02-08-2011 06:28 PM
[NMR paper] Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
Related Articles Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
J Biomol NMR. 2005 Jul;32(3):235-41
Authors: Ozawa K, Jergic S, Crowther JA, Thompson PR, Wijffels G, Otting G, Dixon NA
Cell-free protein synthesis systems provide facile access to proteins in a nascent state that enables formation of soluble, native protein-protein complexes even if one of the protein components is prone...
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12-01-2010 06:56 PM
[NMR paper] NMR studies of protein-ligand interactions.
NMR studies of protein-ligand interactions.
Related Articles NMR studies of protein-ligand interactions.
Methods Mol Biol. 2005;305:197-214
Authors: Maurer T
Interaction between biological macromolecules or of macromolecules with low-molecular-weight ligands is a central paradigm in the understanding of function in biological systems. It is also the major goal in pharmaceutical research to find and optimize ligands that modulate the function of biological macromolecules. Both technological advances and new methods in the field of nuclear...
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11-24-2010 11:14 PM
NMR Studies on Domain Diffusion and Alignment in Modular GB1 Repeats.
NMR Studies on Domain Diffusion and Alignment in Modular GB1 Repeats.
Related Articles NMR Studies on Domain Diffusion and Alignment in Modular GB1 Repeats.
Biophys J. 2010 Oct 20;99(8):2636-46
Authors: Walsh JD, Meier K, Ishima R, Gronenborn AM
Modular proteins contain individual domains that are often connected by flexible, unstructured linkers. Using a model system based on the GB1 domain, we constructed tandem repeat proteins and investigated the rotational diffusion and long-range angular ordering behavior of individual domains by measuring...
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10-22-2010 06:02 AM
[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
Related Articles 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
J Biochem Biophys Methods. 1991 Oct-Nov;23(3):259-61
Authors: YashRoy RC
Spinach chloroplast membranes were studied by natural abundance carbon-13 nuclear magnetic resonance (13C-NMR) spectroscopy in their normal state and after heat denaturation of membrane proteins. The membrane proteins were denatured by raising the temperature of the sample to 67...
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08-21-2010 11:12 PM
[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
Related Articles 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
J Biochem Biophys Methods. 1991 Oct-Nov;23(3):259-61
Authors: YashRoy RC
Spinach chloroplast membranes were studied by natural abundance carbon-13 nuclear magnetic resonance (13C-NMR) spectroscopy in their normal state and after heat denaturation of membrane proteins. The membrane proteins were denatured by raising the temperature of the sample to 67...