Related ArticlesDesign of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR.
Protein Sci. 1997 Nov;6(11):2359-64
Authors: Huth JR, Bewley CA, Jackson BM, Hinnebusch AG, Clore GM, Gronenborn AM
Two protein expression vectors have been designed for the preparation of NMR samples. The vectors encode the immunoglobulin-binding domain of streptococcal protein G (GB1 domain) linked to the N-terminus of the desired proteins. This fusion strategy takes advantage of the small size, stable fold, and high bacterial expression capability of the GB1 domain to allow direct NMR spectroscopic analysis of the fusion protein by 1H-15N correlation spectroscopy. Using this system accelerates the initial assessment of protein NMR projects such that, in a matter of days, the solubility and stability of a protein can be determined. In addition, 15N-labeling of peptides and their testing for DNA binding are facilitated. Several examples are presented that demonstrate the usefulness of this technique for screening protein/DNA complexes, as well as for probing ligand-receptor interactions, using 15N-labeled GB1-peptide fusions and unlabeled target.
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
[NMR paper] Design, expression and solid-state NMR characterization of silk-like materials constr
Design, expression and solid-state NMR characterization of silk-like materials constructed from sequences of spider silk, Samia cynthia ricini and Bombyx mori silk fibroins.
Related Articles Design, expression and solid-state NMR characterization of silk-like materials constructed from sequences of spider silk, Samia cynthia ricini and Bombyx mori silk fibroins.
J Biochem. 2005 Jun;137(6):721-9
Authors: Yang M, Asakura T
Silk has a long history of use in medicine as sutures. To address the requirements of a mechanically robust and...
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11-25-2010 08:21 PM
[NMR paper] Quantitation of protein expression in a cell-free system: Efficient detection of yiel
Quantitation of protein expression in a cell-free system: Efficient detection of yields and 19F NMR to identify folded protein.
Related Articles Quantitation of protein expression in a cell-free system: Efficient detection of yields and 19F NMR to identify folded protein.
J Biomol NMR. 2005 Jan;31(1):11-9
Authors: Neerathilingam M, Greene LH, Colebrooke SA, Campbell ID, Staunton D
We have developed an efficient and novel filter assay method, involving radioactive labelling and imaging, to quantify the expression of soluble proteins from a...
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[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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[NMR paper] An efficient fusion expression system for protein and peptide overexpression in Esche
An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation.
Related Articles An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation.
Protein Pept Lett. 2003 Apr;10(2):175-81
Authors: Cheng Y, Liu D, Feng Y, Jing G
An efficient fusion expression system with a small fusion partner, His6-tagged N-terminal fragment of staphylococcal nuclease R, has been constructed and tested with two genes. The results show that...
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[NMR paper] Design, high-level expression, purification and characterization of soluble fragments
Design, high-level expression, purification and characterization of soluble fragments of the hepatitis C virus NS3 RNA helicase suitable for NMR-based drug discovery methods and mechanistic studies.
Related Articles Design, high-level expression, purification and characterization of soluble fragments of the hepatitis C virus NS3 RNA helicase suitable for NMR-based drug discovery methods and mechanistic studies.
Protein Eng. 2001 Aug;14(8):573-82
Authors: Gesell JJ, Liu D, Madison VS, Hesson T, Wang YS, Weber PC, Wyss DF
RNA helicases represent...
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[NMR paper] Design and NMR analyses of compact, independently folded BBA motifs.
Design and NMR analyses of compact, independently folded BBA motifs.
Related Articles Design and NMR analyses of compact, independently folded BBA motifs.
Fold Des. 1998;3(2):95-103
Authors: Struthers M, Ottesen JJ, Imperiali B
BACKGROUND: Small folded polypeptide motifs represented highly simplified systems for theoretical and experimental studies on protein structure and folding. We have recently reported the design and characterization of a metal-ion-independent 23-residue peptide with a beta beta alpha structure (BBA1), based on the zinc...
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11-17-2010 11:06 PM
[NMR paper] Internal mobility in the partially folded DNA binding and dimerization domains of GAL
Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
Biochemistry. 1996 Feb 27;35(8):2674-86
Authors: Lefevre JF, Dayie KT, Peng JW, Wagner G
The DNA binding domain (residues 1--65) of the yeast transcriptional...
Design of an expression system for detecting folded protein domains and mapping macro
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