Related ArticlesInteraction of the water-soluble protein aprotinin with liposomes: gel-filtration, turbidity studies, and 31P NMR studies.
J Liposome Res. 2003 Nov;13(3-4):213-29
Authors: Tiourina O, Sharf T, Balkina A, Ollivon M, Selischeva A, Sorokoumova G, Larionova N
The interactions of a water-soluble nonmembrane protein aprotinin with multilamellar vesicles (MLV) and small unilamellar vesicles (SUV) from soybean phospholipids were studied using Sephadex G-75 gel chromatography combined with different methods of the analysis of the eluate fractions (fluorescence, light-scattering, turbidity; 31P NMR spectroscopy). The composition of the liposomes mainly containing soybean phosphatidylcholine (PC) was varied by the addition of phosphatidylethanolamine (PE), phosphatidylinositol (PI) and lyso-phosphatidylcholine (lyso-PC). To evaluate the lipid-protein interactions, the amount of aprotinin in the MLV-aprotinin complexes was determined. Lipid-protein interactions were found to strongly depend on the liposome composition, medium pH and ionic strength. These dependencies point to the electrostatic nature of the aprotinin-lipid interactions. 31P NMR spectroscopy of the MLV-aprotinin complexes indicated that aprotinin influences the phospholipid structure in MLV at pH 3.0. In the case of PC:PE:PI and PC:PE:PI:lyso-PC vesicles, aprotinin induced liposome aggregation and a lamellar-to-isotropic phase transition of the phospholipids.
Nmr structure and action on nicotinic acetylcholine receptors of water-soluble domain of human lynx1.
NMR STRUCTURE AND ACTION ON NICOTINIC ACETYLCHOLINE RECEPTORS OF WATER-SOLUBLE DOMAIN OF HUMAN LYNX1.
NMR STRUCTURE AND ACTION ON NICOTINIC ACETYLCHOLINE RECEPTORS OF WATER-SOLUBLE DOMAIN OF HUMAN LYNX1.
J Biol Chem. 2011 Jan 20;
Authors: Lyukmanova EN, Shenkarev ZO, Shulepko MA, Mineev KS, D'Hoedt D, Kasheverov IE, Filkin SY, Krivolapova AP, Janickova H, Dolezal V, Dolgikh DA, Arseniev AS, Bertrand D, Tsetlin VI, Kirpichnikov MP
Discovery of proteins expressed in the central nervous system sharing the three-finger structure with snake...
nmrlearner
Journal club
0
01-22-2011 01:52 PM
[NMR paper] NMR spectroscopic filtration of polypeptides and proteins in complex mixtures.
NMR spectroscopic filtration of polypeptides and proteins in complex mixtures.
Related Articles NMR spectroscopic filtration of polypeptides and proteins in complex mixtures.
J Biomol NMR. 2004 Aug;29(4):505-16
Authors: Rajagopalan S, Chow C, Raghunathan V, Fry CG, Cavagnero S
Due to the inherent complexity of the natural biological environment, most studies on polypeptides, proteins and nucleic acids have so far been performed in vitro, away from physiologically relevant conditions. Nuclear magnetic resonance is an ideal technique to extend...
nmrlearner
Journal club
0
11-24-2010 10:01 PM
[NMR paper] Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fr
Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fragments derived from Paracoccus denitrificans.
Related Articles Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fragments derived from Paracoccus denitrificans.
Biochemistry. 2003 May 27;42(20):6005-12
Authors: Wienk H, Maneg O, Lücke C, Pristovsek P, Löhr F, Ludwig B, Rüterjans H
The functional interactions between the various components of the respiratory chain are relatively short-lived, thus allowing high turnover numbers...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[NMR paper] Multiple quantum filtered NMR studies of the interaction between collagen and water i
Multiple quantum filtered NMR studies of the interaction between collagen and water in the tendon.
Related Articles Multiple quantum filtered NMR studies of the interaction between collagen and water in the tendon.
J Am Chem Soc. 2002 Mar 27;124(12):3125-32
Authors: Eliav U, Navon G
We studied the physical processes and the chemical reactions involved in magnetization transfer between water and large proteins, such as collagen, in bovine Achilles tendon. Since the NMR spectrum for such proteins is broadened by very large dipolar interactions,...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
Efficient protein production method for NMR using soluble protein tags with cold shoc
Efficient protein production method for NMR using soluble protein tags with cold shock expression vector
Abstract The E. coli protein expression system is one of the most useful methods employed for NMR sample preparation. However, the production of some recombinant proteins in E. coli is often hampered by difficulties such as low expression level and low solubility. To address these problems, a modified cold-shock expression system containing a glutathione S-transferase (GST) tag, the pCold-GST system, was investigated. The pCold-GST system successfully expressed 9 out of 10 proteins...
nmrlearner
Journal club
0
09-18-2010 04:53 AM
Efficient protein production method for NMR using soluble protein tags with cold shoc
Efficient protein production method for NMR using soluble protein tags with cold shock expression vector.
Related Articles Efficient protein production method for NMR using soluble protein tags with cold shock expression vector.
J Biomol NMR. 2010 Sep 16;
Authors: Hayashi K, Kojima C
The E. coli protein expression system is one of the most useful methods employed for NMR sample preparation. However, the production of some recombinant proteins in E. coli is often hampered by difficulties such as low expression level and low solubility. To...
Interaction of the water-soluble protein aprotinin with liposomes: gel-filtration, tu
Linear Mode
