[NMR paper] Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.
Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.
Chem Rev. 2018 Feb 28;:
Authors: Chipot C, Dehez F, Schnell JR, Zitzmann N, Pebay-Peyroula E, Catoire LJ, Miroux B, Kunji ERS, Veglia G, Cross TA, Schanda P
Abstract
Membrane proteins perform a host of vital cellular functions. Deciphering the molecular mechanisms whereby they fulfill these functions requires detailed biophysical and structural investigations. Detergents have proven pivotal to extract the protein from its native surroundings. Yet, they provide a milieu that departs significantly from that of the biological membrane, to the extent that the structure, the dynamics, and the interactions of membrane proteins in detergents may considerably vary, as compared to the native environment. Understanding the impact of detergents on membrane proteins is, therefore, crucial to assess the biological relevance of results obtained in detergents. Here, we review the strengths and weaknesses of alkyl phosphocholines (or foscholines), the most widely used detergent in solution-NMR studies of membrane proteins. While this class of detergents is often successful for membrane protein solubilization, a growing list of examples points to destabilizing and denaturing properties, in particular for ?-helical membrane proteins. Our comprehensive analysis stresses the importance of stringent controls when working with this class of detergents and when analyzing the structure and dynamics of membrane proteins in alkyl phosphocholine detergents.
PMID: 29488756 [PubMed - as supplied by publisher]
[NMR paper] Dicarboxylate-Oside Detergents for Extraction, Overstabilization and Crystallization of Membrane Proteins
Dicarboxylate-Oside Detergents for Extraction, Overstabilization and Crystallization of Membrane Proteins
To tackle the problem of membrane proteins (MPs) instability in detergent solutions, we designed a series of dicarboxylate-oside detergents (DCODs) in which we optimized the polar head to clamp the membrane domain, including on one side a cluster of two carboxyl groups that promotes salt-bridges with basic residues abundant at the membrane-cytoplasm interface of MPs, and on the other side a sugar to generate H-bonds. Tested on BmrA, an ATP-binding cassette pump, DCODs 8b, 8c, and 9b...
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[NMR paper] The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013.
The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013.
Related Articles The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013.
J Biomol NMR. 2015 Jun 14;
Authors: Rosato A, Vranken W, Fogh RH, Ragan TJ, Tejero R, Pederson K, Lee HW, Prestegard JH, Yee A, Wu B, Lemak A, Houliston S, Arrowsmith CH, Kennedy M, Acton TB, Xiao R, Liu G, Montelione GT, Vuister GW
Abstract
The second round of the community-wide initiative...
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The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013
The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013
Abstract
The second round of the community-wide initiative Critical Assessment of automated Structure Determination of Proteins by NMR (CASD-NMR-2013) comprised ten blind target datasets, consisting of unprocessed spectral data, assigned chemical shift lists and unassigned NOESY peak and RDC lists, that were made available in both curated (i.e. manually refined) or un-curated (i.e. automatically generated) form. Ten structure calculation...
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
J Biol Chem. 2011 Jul 28;
Authors: Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS
Subcellular distribution of Calmodulin (CaM) in human immunodeficiency virus type-1 (HIV-1) infected cells is distinct from that observed in uninfected cells. CaM has been shown to interact and co-localize with the HIV-1 Gag protein...
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07-30-2011 11:23 AM
[NMR paper] An evaluation of detergents for NMR structural studies of membrane proteins.
An evaluation of detergents for NMR structural studies of membrane proteins.
Related Articles An evaluation of detergents for NMR structural studies of membrane proteins.
J Biomol NMR. 2004 Jan;28(1):43-57
Authors: Krueger-Koplin RD, Sorgen PL, Krueger-Koplin ST, Rivera-Torres IO, Cahill SM, Hicks DB, Grinius L, Krulwich TA, Girvin ME
Structural information on membrane proteins lags far behind that on soluble proteins, in large part due to difficulties producing homogeneous, stable, structurally relevant samples in a membrane-like environment....
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11-24-2010 09:25 PM
[NMR paper] 19F NMR study of protein-induced rhombic perturbations on the electronic structure of
19F NMR study of protein-induced rhombic perturbations on the electronic structure of the active site of myoglobin.
Related Articles 19F NMR study of protein-induced rhombic perturbations on the electronic structure of the active site of myoglobin.
J Biol Inorg Chem. 2000 Aug;5(4):455-62
Authors: Yamamoto Y, Hirai Y, Suzuki A
A novel C2-symmetric ring-fluorinated hemin, 13,17-bis(2-carboxyethyl)-2,8,12,18-tetramethyl-3,7-difluoroporphyrin atoiron(III), has been synthesized and was incorporated into sperm whale apomyoglobin to investigate...
Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.
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