Related ArticlesContemporary NMR Studies of Protein Electrostatics.
Annu Rev Biophys. 2015 Feb 26;
Authors: Hass MA, Mulder FA
Abstract
Electrostatics play an important role in many aspects of protein chemistry. However, the accurate determination of side chain proton affinity in proteins by experiment and theory remains challenging. In recent years the field of nuclear magnetic resonance spectroscopy has advanced the way that protonation states are measured, allowing researchers to examine electrostatic interactions at an unprecedented level of detail and accuracy. Experiments are now in place that follow pH-dependent (13)C and (15)N chemical shifts as spatially close as possible to the sites of protonation, allowing all titratable amino acid side chains to be probed sequence specifically. The strong and telling response of carefully selected reporter nuclei allows individual titration events to be monitored. At the same time, improved frameworks allow researchers to model multiple coupled protonation equilibria and to identify the underlying pH-dependent contributions to the chemical shifts. Expected final online publication date for the Annual Review of Biophysics Volume 44 is May 06, 2015. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.
PMID: 25747592 [PubMed - as supplied by publisher]
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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[NMR paper] NMR studies for identifying phosphopeptide ligands of the HIV-1 protein Vpu binding to the F-box protein beta-TrCP.
NMR studies for identifying phosphopeptide ligands of the HIV-1 protein Vpu binding to the F-box protein beta-TrCP.
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Peptides. 2006 Jan;27(1):194-210
Authors: Evrard-Todeschi N, Gharbi-Benarous J, Bertho G, Coadou G, Megy S, Benarous R, Girault JP
The human immunodeficiency virus type 1 (HIV-1) Vpu enhances viral particle release and, its interaction with the ubiquitin ligase SCF-beta-TrCP triggers the HIV-1...
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[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.
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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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[NMR paper] Studies of protein-protein association between yeast cytochrome c peroxidase and yeas
Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy.
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Biochemistry. 1994 Oct 11;33(40):12032-41
Authors: Yi Q, Erman JE, Satterlee JD
Hydrogen-deuterium (H-D) exchange labeling and proton NMR have been applied to study the...
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[NMR paper] Relationship between electrostatics and redox function in human thioredoxin: characte
Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR.
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Biochemistry. 1992 Apr 7;31(13):3442-52
Authors: Forman-Kay JD, Clore GM, Gronenborn AM
The electrostatic behavior of potentially titrating groups in reduced human thioredoxin was investigated...
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[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
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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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[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
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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...
Contemporary NMR Studies of Protein Electrostatics.
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