Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
J Phys Chem B. 2011 Jun 8;
Authors: Breen NF, Li K, Olsen GL, Drobny GP
LK?14 is a 14 amino acid peptide which displays a periodic alternation of leucine and lysine amino acids. This "hydrophobic periodicity" has been found to result in an ?-helical secondary structure...
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06-10-2011 11:52 AM
[NMR paper] Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote
Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
Related Articles Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
Peptides. 2002 Dec;23(12):2127-41
Authors: de Chiara C, Nicastro G, Spisni A, Zanotti F, Cocco T, Papa S
The protein IF(1) is a natural inhibitor of the mitochondrial F(o)F(1)-ATPase. Many investigators have been prompted to identify the shortest segment of IF(1), retaining its native activity, for use in biomedical applications. Here, the...
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11-24-2010 08:58 PM
[NMR paper] Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectrosc
Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy.
Related Articles Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy.
Biochemistry. 2001 Feb 20;40(7):1884-9
Authors: Rohrer M, Prisner TF, Brügmann O, Käss H, Spoerner M, Wittinghofer A, Kalbitzer HR
The small GTPase Ras plays a key role as a molecular switch in the intercellular signal transduction. On Mg(2+) --> Mn(2+) substituted samples, the first ligand sphere of...
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11-19-2010 08:32 PM
[NMR paper] Probing membrane surfaces and the location of membrane-embedded peptides by (13)C MAS
Probing membrane surfaces and the location of membrane-embedded peptides by (13)C MAS NMR using lanthanide ions.
Related Articles Probing membrane surfaces and the location of membrane-embedded peptides by (13)C MAS NMR using lanthanide ions.
J Magn Reson. 1999 Dec;141(2):335-9
Authors: Gröbner G, Glaubitz C, Watts A
A simple but efficient (13)C MAS NMR method is presented for the determination of the location of embedded molecules such as peptides relative to biological membrane surfaces by exploiting the interaction with paramagnetic...
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11-18-2010 08:31 PM
[NMR paper] 1H NMR studies on the CuA center of nitrous oxide reductase from Pseudomonas stutzeri
1H NMR studies on the CuA center of nitrous oxide reductase from Pseudomonas stutzeri.
Related Articles 1H NMR studies on the CuA center of nitrous oxide reductase from Pseudomonas stutzeri.
Biochemistry. 1999 Aug 24;38(34):11164-71
Authors: Holz RC, Alvarez ML, Zumft WG, Dooley DM
1H NMR spectra of the CuA center of N2OR from Pseudomonas stutzeri, and a mutant enzyme that contains only CuA, were recorded in both H2O- and D2O-buffered solution at pH 7.5. Several sharp, well-resolved hyperfine-shifted 1H NMR signals were observed in the 60 to...
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[NMR paper] NMR structure and metal interactions of the CopZ copper chaperone.
NMR structure and metal interactions of the CopZ copper chaperone.
Related Articles NMR structure and metal interactions of the CopZ copper chaperone.
J Biol Chem. 1999 Aug 6;274(32):22597-603
Authors: Wimmer R, Herrmann T, Solioz M, Wüthrich K
A recently discovered family of proteins that function as copper chaperones route copper to proteins that either require it for their function or are involved in its transport. In Enterococcus hirae the copper chaperone function is performed by the 8-kDa protein CopZ. This paper describes the NMR...
[NMR paper] Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region o
Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.
J Biol Chem. 1995 Apr 7;270(14):7980-7
Authors: Freedman SJ, Furie BC, Furie B, Baleja JD
The gamma-carboxyglutamic acid-rich...
Structure of Peptides on Metal Oxide Surfaces Probed by NMR
Linear Mode
