Related Articles2H NMR studies of a myristoylated peptide in neutral and acidic phospholipid bicelles.
Biochemistry. 1998 Nov 3;37(44):15523-7
Authors: Struppe J, Komives EA, Taylor SS, Vold RR
Deuterium NMR spectra of Myr-d27-GNAAAAKKGSEQES (Cat14), the N-terminal 14-residue peptide from the catalytic subunit of cAMP-dependent protein kinase A (PKA), illustrate how magnetically aligned neutral and acidic phospholipid bicelles can be used to characterize the ordering and mode of binding of peptides to membranes. Since Cat14 is electrically neutral, the major interaction responsible for binding is the insertion of the myristoyl group into the hydrophobic core of the bilayer. The inclusion of 25% phosphatidylserine or phosphatidylglycerol into phosphatidylcholine bicelles results in a moderate increase in the ordering of the peptide relative to the bicelle normal, presumably because of favorable electrostatic interactions between the phospholipid headgroups and the two lysines in positions 7 and 8. Successful preparation of acidic bicelles was achieved by careful adjustment of lipid composition, pH and ionic strength.
Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
J Phys Chem B. 2011 Sep 22;
Authors: Yamamoto K, Vivekanandan S, Ramamoorthy A
Abstract
In spite of recent technological advances in NMR spectroscopy, its low sensitivity continues to be a major limitation particularly for the structural studies of membrane proteins. The need for a large quantity of a membrane protein and acquisition of...
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09-24-2011 04:11 PM
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] 15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth fa
15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth factor.
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J Biol Chem. 2000 Dec 15;275(50):39444-50
Authors: Chi Y, Kumar TK, Chiu IM, Yu C
15N NMR relaxation data have been used to characterize the backbone dynamics of the human acidic fibroblast growth factor (hFGF-1) in its free and sucrose octasulfate (SOS)-bound states. (15)N longitudinal (R(1)), transverse (R(2)) relaxation rates and (1H)-(15)N...
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11-19-2010 08:29 PM
[NMR paper] H-NMR and CD studies on the structural transition of serum albumin in the acidic regi
H-NMR and CD studies on the structural transition of serum albumin in the acidic region--the N-->F transition.
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J Pept Res. 1998 Dec;52(6):431-42
Authors: Era S, Sogami M
Helical content (f(alpha)) of bovine mercaptalbumin (BMA) showed the characteristic two-step decrease in the acidic region, one corresponding to the N-->F transition (pH 4.40-->3.75; f(alpha), 0.68-->0.58) and the other to the F-->E transition (the...
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11-17-2010 11:15 PM
[NMR paper] Solid-state NMR studies of magnetically aligned phospholipid membranes: taming lantha
Solid-state NMR studies of magnetically aligned phospholipid membranes: taming lanthanides for membrane protein studies.
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Biochem Cell Biol. 1998;76(2-3):443-51
Authors: Prosser RS, Volkov VB, Shiyanovskaya IV
The addition of lanthanides (Tm3+, Yb3+, Er3+, or Eu3+) to a solution of long-chain phospholipids such as dimyristoylphosphatidylcholine (DMPC) and short-chain phospholipids such as...
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[NMR paper] Structural studies of the acidic transactivation domain of the Vmw65 protein of herpe
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Biochemistry. 1992 Apr 28;31(16):4150-6
Authors: O'Hare P, Williams G
We have overproduced and purified the carboxy-terminal transactivation domain of Vmw65 (VP16) of herpes simplex virus, and studied potential folding of the domain by 1H NMR. Two species of the acidic domain were obtained from the...
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08-21-2010 11:41 PM
[NMR paper] Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: s
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Biochemistry. 1991 Dec 10;30(49):11600-8
Authors: Simorre JP, Caille A, Marion D, Marion D, Ptak M
Two- and three-dimensional 1H NMR experiments have been used to sequentially assign nearly all proton resonances of the 90 residues of wheat...
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[NMR paper] Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: s
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Biochemistry. 1991 Dec 10;30(49):11600-8
Authors: Simorre JP, Caille A, Marion D, Marion D, Ptak M
Two- and three-dimensional 1H NMR experiments have been used to sequentially assign nearly all proton resonances of the 90 residues of wheat...
2H NMR studies of a myristoylated peptide in neutral and acidic phospholipid bicelles
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