Membrane Proteins

Membrane proteins make up between 20% and 30% of all expressed proteins and are medically important, as they represent more than half of all present-day drug targets. Membrane proteins have hydrophobic exteriors, are relatively dynamic, and are produced at relatively low levels. These factors create difficulties in obtaining stable preparations for NMR analyses. Despite the significant functional importance of membrane proteins, determining structures for these proteins is much more challenging than for globular proteins. Fortunately, there are many sample preparation conditions that can be chosen for solution and solid state NMR. Most preparations require a detergent or phospholipid for proper solubilization and stability. In this regard, Cambridge Isotope Laboratories is pleased to be able to offer deuterated phospholipids and detergents from FB Reagents, Ltd., a trusted source for deuterated lipids.

The study of structure, dynamics, and small molecule binding properties of membrane proteins are of great interest within the field of Structural Biology and pharmaceutical drug development. The study of membrane proteins is made challenging because only certain phospholipids and detergents can be used to ensure the protein assumes the correct three dimensional fold and remains active. Cambridge Isotope Laboratories, Inc. is proud to offer deuterated phospholipids and detergents manufactured by FB Reagents. FB Reagents is a trusted source of high quality deuterated phospholipids and detergents used in NMR-based scientific research.

Deuterated Phospholipids

The study of structure, dynamics, and small-molecule binding properties of membrane proteins are of great interest within the field of structural biology and pharmaceutical drug development. The study of membrane proteins is made challenging because only certain phospholipids and detergents can be used to ensure the protein assumes the correct three-dimensional fold and remains active. Cambridge Isotope Laboratories, Inc. is proud to offer deuterated phospholipids and detergents manufactured by FB Reagents. FB Reagents is a trusted source of high-quality deuterated phospholipids and detergents used in NMR-based scientific research.
The benefits for using highly deuterated phospholipids are:
  • Simplification of 1H-NMR spectrum
  • Easier detection of signals from biomolecules in multidimensional NMR experiments
  • Minimization of dipolar relaxation effects leads to signal enhancement in certain systems
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Item No. Description Acronym Size
DLM-11085
1,2-Dihexanoyl-sn-glycero-3-phosphocholine
(hexanoyl-D22, 97%; 50-60% on alpha carbons)
 DH6PC-d22 100 mg
DLM-11092
1,2-Diheptanoyl-sn-glycero-3-phosphocholine
(heptanoyl-D26, 97%; 50-60% on alpha carbons)
 DH7PC-d26 100 mg
DLM-11094
1,2-Dipalmitoyl-sn-glycero-3-phosphocholine
(dipalmitoyl-D62, 97%; 50-60% on alpha carbons)
 DPPC-d62 100 mg
DLM-11095
1,2-Dioleoyl-sn-glycero-3-phosphocholine
(dioleoyl-D64, 97%; 50-60% on alpha, vinyl carbons)
 DOPC-d64 50 mg
DLM-11096
1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
(fatty acids-D63, 97%; 50-60% on alpha, vinyl carbons)
 POPC-d63 50 mg
DLM-11097
1,2-Dimyristoyl-sn-glycero-3-phosphoglycerol, NH4+
(dimyristoyl-D54, 97%; 50-60% on alpha carbons)
 DMPG-d54 100 mg
DLM-11098
1,2-Dipalmitoyl-sn-glycero-3-phosphoethanolamine
(dipalmitoyl-D62, 97%; 50-60% at alpha carbon)
 DPPE-d62 100 mg
DLM-11099
1,2-Dipalmitoyl-sn-glycero-3-phosphoserine, NH4+
(dipalmitoyl-D62, 97%; 50-60% on alpha carbons)
 DPPS-d62 50 mg
DLM-11100
1-Myristoyl-2-lyso-sn-glycero-3-phosphoglycerol NH4+
(myristoyl-D27, 97%; 50-60% at alpha carbon)
 LMPG-d27 100 mg
DLM-11101
1-Palmitoyl-2-lyso-sn-glycero-3-phosphoglycerol NH4+
(palmitoyl-D31, 97%; 50-60% at alpha carbon)
 LPPG-d31 100 mg
DLM-11102
Lauryl-N,N-dimethyl N-oxide
(lauryl-D25; dimethylamine-D6, 97%)
 LDAO-d31 100 mg
DLM-11103 Dodecyl-β-D-maltopyranoside (dodecyl-D25, 97%) DDM-d25 100 mg
DLM-11104
Decanoyl-rac-glycerol
(decanoyl-D19, glycerol-D5, 97% (50-60% on alpha)
 10-MAG-d24 100 mg
DLM-11105 L-α-Glycerophosphocholine-d9 (methyl-D9, 97%) GPC-d9 100 mg

References

  1. Movelan, K.T.; Wegstroth, M.; Overkamp, K.; et al. 2020. Imidazole-imidazole hydrogen bonding in the pH-densing histidine side chains of influenza A M2. J Am Chem Soc, 142(6), 2704-2708. PMID: 31970979
  2. Bibow, S. 2019. Opportunities and challenges of backbone, sidechain and RDC experiments to study membrane protein dynamics in a detergent-free lipid environment using solution state NMR. Front Mol Biosci, 6, 103. PMID: 31709261
  3. Eddy, M.T.; Yu, T.Y.; Wagner, G.; et al. 2019. Structural characterization of the human membrane protein VDAC2 in lipid bilayers by MAS NMR. J Biomol NMR, 73(8-9), 451-460. PMID: 31407201
  4. Bayrhuber, M.; Maslennikov, I.; Kwiatkowski, W.; et al.  2019. NMR solution structure and functional behavior of the human proton channel. Biochemistry, 58(39), 4017-4027. PMID: 31365236
  5. Toyama, Y.; Shimada, I. 2019. Frequency selective coherence transfer NMR spectroscopy to study the structural dynamics of high molecular weight proteins. J Mag Res, 304, 62-67. PMID: 31129430
  6. Brazin, K.N.; Mallis, R.J.; Boeszoermenyi, A.; et al. 2018. The T cell antigen receptor a transmembrane domain coordinates triggering through regulation of bilayer immersion and CD3 subunit associations. Immunity, 49(5), 829-841. PMID: 30389415
  7. O’Brien, E.S.; Lin, D.W.; Fuglestad, B.; et al. 2018. Improving yields of deuterated, methyl labeled protein by growing in H2O. J Biomol NMR, 71(4), 263-273 . PMID: 30073492
  8. Hagn, F.; Nasr, M.L.; Wagner, G. 2018. Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR. Nat Protoc, 13(1), 79-98. PMID: 29215632
  9. Arenas, R.C.; Danielczak, B.; Martel, A.; et al. 2017. Fast collisional lipid transfer among polymer-bounded nanodiscs. Scientific Reports, 7, 45875. PMID: 28378790
  10. Bibow, S.; Polyhach, Y.; Eichmann, C.; et al. 2017. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I. Nat Struct Mol Biol, 24(24), 187-193. PMID: 28024148
  11. Laguerre, A.; Lõhr, F.; Henrich, E.; et al. 2016. From nanodiscs to isotropic bicelles: a procedure for solution NMR studies of detergent sensitive integral membrane proteins. Structure, 24(10), 1830-1841. PMID: 27618661
  12. Bugge, K.; Papaleo, E.; Haxholm, G.W.; et al. 2016. A combined computational and structural model of the full-length human prolactin receptor. Nat Commun, 7, 11578. PMID: 27174498
  13. Hagn, F.; Etzkorn, M.; Raschle, T.; et al. 2013. Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins. J Am Chem Soc, 135(5), 1919-1925. PMID: 23294159

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