Related ArticlesIdentification and optimization of protein domains for NMR studies.
Methods Enzymol. 2005;394:3-16
Authors: Card PB, Gardner KH
The success of genomic sequencing projects in recent years has presented protein scientists with a formidable challenge in characterizing the vast number of gene products that have subsequently been identified. NMR has proven to be a valuable tool in the elucidation of various properties for many of these proteins, allowing versatile studies of structure, dynamics, and interactions in the solution state. But the characteristics needed for proteins amenable to this kind of study, such as folding capability, long-term stability, and high solubility, require robust and expeditious methods for the identification and optimization of target protein domains. Here we present a variety of computational and experimental methods developed for these purposes and show that great care must often be taken in the design of constructs intended for NMR-based investigations.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Protein Expr Purif. 2011 Feb 11;
Authors: Wang X, Gill Jr RL, Zhu Q, Tian F
LR11 (SorLA) is a recently identified neuronal protein that interacts with amyloid precursor protein (APP), a central player...
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02-16-2011 07:40 PM
FM reconstruction of non-uniformly sampled protein NMR data at higher dimensions and optimization by distillation
FM reconstruction of non-uniformly sampled protein NMR data at higher dimensions and optimization by distillation
Abstract Non-uniform sampling (NUS) enables recording of multidimensional NMR data at resolutions matching the resolving power of modern instruments without using excessive measuring time. However, in order to obtain satisfying results, efficient reconstruction methods are needed. Here we describe an optimized version of the Forward Maximum entropy (FM) reconstruction method, which can reconstruct up to three indirect dimensions. For complex datasets, such as NOESY spectra,...
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01-09-2011 12:46 PM
[NMR paper] Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors.
Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors.
Related Articles Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors.
Chembiochem. 2005 Sep;6(9):1607-10
Authors: Jahnke W, Blommers MJ, Fernández C, Zwingelstein C, Amstutz R
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[NMR paper] NMR structural comparison of the cytoplasmic juxtamembrane domains of G-protein-coupl
NMR structural comparison of the cytoplasmic juxtamembrane domains of G-protein-coupled CB1 and CB2 receptors in membrane mimetic dodecylphosphocholine micelles.
Related Articles NMR structural comparison of the cytoplasmic juxtamembrane domains of G-protein-coupled CB1 and CB2 receptors in membrane mimetic dodecylphosphocholine micelles.
J Biol Chem. 2005 Feb 4;280(5):3605-12
Authors: Xie XQ, Chen JZ
The fourth cytoplasmic domain, the so-called C-terminal juxtamembrane segment or helix VIII, has been identified in numerous G-protein-coupled...
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11-24-2010 10:03 PM
[NMR paper] Expression screening, protein purification and NMR analysis of human protein domains
Expression screening, protein purification and NMR analysis of human protein domains for structural genomics.
Related Articles Expression screening, protein purification and NMR analysis of human protein domains for structural genomics.
J Struct Funct Genomics. 2004;5(1-2):119-31
Authors: Folkers GE, van Buuren BN, Kaptein R
Structural genomics, the determination of protein structures on a genome-wide scale, is still in its infancy for eukaryotes due to the number and size of their genes. Low protein expression and solubility of eukaryotic...
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11-24-2010 09:25 PM
[NMR paper] Crystal structure and NMR studies of the apo SH2 domains of ZAP-70: two bikes rather
Crystal structure and NMR studies of the apo SH2 domains of ZAP-70: two bikes rather than a tandem.
Related Articles Crystal structure and NMR studies of the apo SH2 domains of ZAP-70: two bikes rather than a tandem.
Biochemistry. 2002 Dec 3;41(48):14176-84
Authors: Folmer RH, Geschwindner S, Xue Y
The protein kinase ZAP-70 is involved in T-cell activation, and interacts with tyrosine-phosphorylated peptide sequences known as immunoreceptor tyrosine activation motifs (ITAMs), which are present in three of the subunits of the T-cell receptor....
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11-24-2010 08:58 PM
[NMR paper] NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing regio
NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing region of the epithelial sodium channel.
Related Articles NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing region of the epithelial sodium channel.
Biochem Cell Biol. 1998;76(2-3):341-50
Authors: Kanelis V, Farrow NA, Kay LE, Rotin D, Forman-Kay JD
Nedd4 (neuronal precursor cell-expressed developmentally down-regulated 4) is a ubiquitin-protein ligase containing multiple WW domains. We have previously demonstrated the association...
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11-17-2010 11:06 PM
[NMR paper] The identification of cation-binding domains on the surface of microsomal cytochrome
The identification of cation-binding domains on the surface of microsomal cytochrome b5 using 1H-NMR paramagnetic difference spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The identification of cation-binding domains on the surface of microsomal cytochrome b5 using 1H-NMR paramagnetic difference spectroscopy.
Eur J Biochem. 1992 Jan 15;203(1-2):211-23
Authors: Whitford D
One-dimensional and two-dimensional 1H-NMR...
Identification and optimization of protein domains for NMR studies.
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