Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Abstract Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties with achieving proper folding, membrane insertion, and native-like post-translational modifications frequently disqualify bacterial expression systems. On the other hand, eukaryotic cell cultures can be prohibitively expensive. One of the viable alternatives,...
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01-22-2011 03:46 AM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
J Biomol NMR. 2011 Jan 19;
Authors: Fan Y, Shi L, Ladizhansky V, Brown LS
Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties...
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01-21-2011 01:22 AM
[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...
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11-24-2010 09:51 PM
[NMR paper] NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformation
NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.
Related Articles NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.
J Biol Chem. 2004 Aug 13;279(33):34963-70
Authors: Santiveri CM, Pérez-Cañadillas JM, Vadivelu MK, Allen MD, Rutherford TJ, Watkins NA, Bycroft M
The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free alpha-hemoglobin, has been determined using NMR spectroscopy....
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11-24-2010 09:51 PM
[NMR paper] The membrane-bound conformation of alpha-lactalbumin studied by NMR-monitored 1H exch
The membrane-bound conformation of alpha-lactalbumin studied by NMR-monitored 1H exchange.
Related Articles The 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...
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11-24-2010 08:58 PM
[NMR paper] Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through
Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
Related Articles Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
J Biol Chem. 1998 Oct 16;273(42):27357-63
Authors: McInnes C, Wang J, Al Moustafa AE, Yansouni C, O'Connor-McCourt M, Sykes BD
The investigation of a...
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11-17-2010 11:15 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...
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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...
NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
Linear Mode
