[NMR paper] Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Related Articles Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
J Am Chem Soc. 2005 Sep 28;127(38):13110-1
Authors: Soubias O, Gawrisch K
We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR). The results indicate a strong preference for interaction of rhodopsin with the...
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12-01-2010 06:56 PM
[NMR paper] A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
Related Articles A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
J Biol Chem. 2005 Nov 18;280(46):38259-63
Authors: Banci L, Bertini I, Cantini F, Chasapis CT, Hadjiliadis N, Rosato A
ATP7A is a P-type ATPase involved in copper(I) homeostasis in humans. It possesses a long N-terminal tail protruding into the cytosol and containing six...
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12-01-2010 06:56 PM
[NMR paper] An NMR study of the interaction between the human copper(I) chaperone and the second
An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
Related Articles An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
FEBS J. 2005 Feb;272(3):865-71
Authors: Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A
The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein...
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11-24-2010 11:14 PM
[NMR paper] Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II),
Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies.
Related Articles Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies.
J Am Chem Soc. 2005 Jan 26;127(3):996-1006
Authors: Gaggelli E, Bernardi F, Molteni E, Pogni R, Valensin D, Valensin G, Remelli M, Luczkowski M, Kozlowski H
The synthetic peptide encompassing residues 106-126 (PrP106-126, KTNMKHMAGAAAAGAVVGGLG) of the human prion protein was considered for...
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11-24-2010 11:14 PM
[NMR paper] X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillu
X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillus subtilis: the coordination properties of the copper ion.
Related Articles X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillus subtilis: the coordination properties of the copper ion.
Biochemistry. 2003 Mar 4;42(8):2467-74
Authors: Banci L, Bertini I, Del Conte R, Mangani S, Meyer-Klaucke W
XAS studies have been performed, under various experimental conditions, on a copper(I)-transporting protein, CopZ, of Bacillus subtilis....
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11-24-2010 09:01 PM
[NMR paper] Probing proteins in solution by (129)Xe NMR spectroscopy.
Probing proteins in solution by (129)Xe NMR spectroscopy.
Related Articles Probing proteins in solution by (129)Xe NMR spectroscopy.
J Magn Reson. 2001 Jun;150(2):167-74
Authors: Locci E, Dehouck Y, Casu M, Saba G, Lai A, Luhmer M, Reisse J, Bartik K
The interaction of xenon with different proteins in aqueous solution is investigated by (129)Xe NMR spectroscopy. Chemical shifts are measured in horse metmyoglobin, hen egg white lysozyme, and horse cytochrome c solutions as a function of xenon concentration. In these systems, xenon is in fast...
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11-19-2010 08:32 PM
[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...
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11-18-2010 08:31 PM
[NMR paper] NMR solution structure of a cytoplasmic surface loop of the human red cell anion tran
NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.
Related Articles NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.
Biochemistry. 1998 Aug 18;37(33):11670-8
Authors: Askin D, Bloomberg GB, Chambers EJ, Tanner MJ
The membrane domain of the human red cell anion transport protein, band 3, is too large to be studied by solution nuclear magnetic resonance spectroscopy (NMR), and its amphiphilic nature requires the use of detergents for...
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Linear Mode
