Related ArticlesThe membrane-bound conformation of alpha-lactalbumin studied by NMR-monitored 1H exchange.
J Mol Biol. 2002 Aug 2;321(1):99-110
Authors: Halskau Ø, Frøystein NA, Muga A, Martínez A
The interaction of bovine alpha-lactalbumin (BLA) with negatively charged phospholipid bilayers was studied by NMR monitored 1H exchange to characterize the conformational transition that enables a water-soluble protein to associate with and partially insert into a membrane. BLA was allowed to exchange in deuterated buffer in the absence (reference) and the presence (membrane-bound) of acidic liposomes at pH 4.5, experimental conditions that allow efficient protein-membrane interaction. After adjusting the pH to 6.0, to dissociate the protein from the membrane, reference and membrane-released samples of BLA were analysed by (F1) band-selective homonuclear decoupled total correlation spectroscopy in the alphaH-NH region. The overall exchange behaviour of the membrane-bound state is molten globule-like, suggesting an overall destabilization of the polypeptide. Nevertheless, the backbone amide protons of residues R10, L12, C77, K94, K98, V99 and W104 show significant protection against solvent exchange in the membrane-bound protein. We propose a mechanism for the association of BLA with negatively charged membranes that includes initial protonation of acidic side-chains at the membrane interface, and formation of an interacting site with the membrane which involves helixes A and C. In the next step these helices would slide away from each other, adopting a parallel orientation to the membrane, and would rotate to maximize the interaction between their hydrophobic residues and the lipid bilayer.
[NMR paper] How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Related Articles How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Chembiochem. 2005 Sep;6(9):1693-700
Authors: Lorch M, Faham S, Kaiser C, Weber I, Mason AJ, Bowie JU, Glaubitz C
Several studies have demonstrated that it is viable to use microcrystalline preparations of water-soluble proteins as...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Related Articles Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Biochemistry. 2005 May 31;44(21):7644-55
Authors: Laurents DV, Scholtz JM, Rico M, Pace CN, Bruix M
The conformational stability of ribonuclease Sa (RNase Sa) has been measured at the per-residue level by NMR-monitored hydrogen exchange at pH* 5.5 and 30 degrees C. In these conditions, the exchange mechanism was found to be EXII. The conformational stability...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[NMR paper] Adsorption of bovine alpha-lactalbumin on suspended solid nanospheres and its subsequ
Adsorption of bovine alpha-lactalbumin on suspended solid nanospheres and its subsequent displacement studied by NMR spectroscopy.
Related Articles Adsorption of bovine alpha-lactalbumin on suspended solid nanospheres and its subsequent displacement studied by NMR spectroscopy.
Langmuir. 2004 Jun 22;20(13):5530-8
Authors: Engel MF, Visser AJ, van Mierlo CP
Detailed knowledge of the adsorption-induced conformational changes of proteins is essential to understand the process of protein adsorption. However, not much information about these...
nmrlearner
Journal club
0
11-24-2010 09:51 PM
[NMR paper] Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined b
Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR.
Related Articles Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR.
Protein Sci. 1998 Sep;7(9):1930-8
Authors: Kim S, Baum J
alpha-Lactalbumin (alpha-LA) undergoes a pH-dependent unfolding from the native state to a partially unfolded state (the molten globule state). To understand the role of electrostatic interactions in protein denaturation, NMR and CD pH titration experiments are performed on guinea pig...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Cadmium-113 NMR studies of bovine and human alpha-lactalbumin and equine lysozyme.
Cadmium-113 NMR studies of bovine and human alpha-lactalbumin and equine lysozyme.
Related Articles Cadmium-113 NMR studies of bovine and human alpha-lactalbumin and equine lysozyme.
J Biochem. 1995 Mar;117(3):623-8
Authors: Aramini JM, Hiraoki T, Ke Y, Nitta K, Vogel HJ
The high-affinity calcium-binding sites of bovine and human alpha-lactalbumin as well as equine lysozyme were analyzed by 113Cd NMR spectroscopy. In the case of equine lysozyme, the addition of isotopically enriched 113Cd2+ results in a signal at delta = -75.9 ppm...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] NMR studies of [U-13C]cyclosporin A bound to cyclophilin: bound conformation and port
NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Related Articles NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Biochemistry. 1991 Jul 2;30(26):6574-83
Authors: Fesik SW, Gampe RT, Eaton HL, Gemmecker G, Olejniczak ET, Neri P, Holzman TF, Egan DA, Edalji R, Simmer R
Cyclosporin A (CsA), a potent immunosuppressant, is known to bind with high specificity to cyclophilin (CyP), a 17.7 kDa protein with...
nmrlearner
Journal club
0
08-21-2010 11:12 PM
[NMR paper] NMR studies of [U-13C]cyclosporin A bound to cyclophilin: bound conformation and port
NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Related Articles NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Biochemistry. 1991 Jul 2;30(26):6574-83
Authors: Fesik SW, Gampe RT, Eaton HL, Gemmecker G, Olejniczak ET, Neri P, Holzman TF, Egan DA, Edalji R, Simmer R
Cyclosporin A (CsA), a potent immunosuppressant, is known to bind with high specificity to cyclophilin (CyP), a 17.7 kDa protein with...
nmrlearner
Journal club
0
08-21-2010 11:12 PM
[NMR paper] NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
Related Articles NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
Basic Life Sci. 1990;56:231-53
Authors: Berliner LJ, Kaptein R, Koga K, Musci G