Related ArticlesMicrodrop screening: a rapid method to optimize solvent conditions for NMR spectroscopy of proteins.
J Biomol NMR. 1998 Nov;12(4):493-9
Authors: Lepre CA, Moore JM
Determining appropriate solvent conditions is a crucial first step for carrying out NMR spectroscopy of proteins, but rapid and efficient methods for doing so are currently lacking. Microdrop screening examines a large number of different solvent conditions using very small amounts of protein and minimal labor. Starting from one initial buffer condition, small aliquots of protein solution are combined with an array of solutions in which concentration, pH, buffer type, and added stabilizers are systematically varied. The protein concentration of each microliter-sized test drop ('microdrop') is gradually changed using vapor diffusion, and the solubility of the protein is determined by visual examination. A variety of analytical techniques may be applied to the contents of the microdrops to monitor enzymatic activity, aggregation, ligand binding, and protein folding.
Rapid acquisition of (1) H and (19) F NMR experiments for direct and competition ligand-based screening.
Rapid acquisition of (1) H and (19) F NMR experiments for direct and competition ligand-based screening.
Rapid acquisition of (1) H and (19) F NMR experiments for direct and competition ligand-based screening.
Magn Reson Chem. 2011 Mar 9;
Authors: Dalvit C, Gossert AD, Coutant J, Piotto M
Direct and competition ligand-based NMR experiments are often used in the screening of chemical fragment libraries against a protein target due to the high relative sensitivity of NMR for protein-binding events. A plethora of NMR methods has been proposed...
[NMR paper] TINS, target immobilized NMR screening: an efficient and sensitive method for ligand
TINS, target immobilized NMR screening: an efficient and sensitive method for ligand discovery.
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Chem Biol. 2005 Feb;12(2):207-16
Authors: Vanwetswinkel S, Heetebrij RJ, van Duynhoven J, Hollander JG, Filippov DV, Hajduk PJ, Siegal G
We propose a ligand screening method, called TINS (target immobilized NMR screening), which reduces the amount of target required for the fragment-based approach to drug discovery. Binding is detected by...
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[NMR paper] ALARM NMR: a rapid and robust experimental method to detect reactive false positives
ALARM NMR: a rapid and robust experimental method to detect reactive false positives in biochemical screens.
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J Am Chem Soc. 2005 Jan 12;127(1):217-24
Authors: Huth JR, Mendoza R, Olejniczak ET, Johnson RW, Cothron DA, Liu Y, Lerner CG, Chen J, Hajduk PJ
High-throughput screening (HTS) of large compound collections typically results in numerous small molecule hits that must be carefully evaluated to identify valid drug...
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[NMR paper] A general NMR method for rapid, efficient, and reliable biochemical screening.
A general NMR method for rapid, efficient, and reliable biochemical screening.
Related Articles A general NMR method for rapid, efficient, and reliable biochemical screening.
J Am Chem Soc. 2003 Nov 26;125(47):14620-5
Authors: Dalvit C, Ardini E, Flocco M, Fogliatto GP, Mongelli N, Veronesi M
High-throughput screening is usually the method of drug-lead discovery. It is now well accepted that, for a functional assay, quality is more important than quantity. The ligand-based or protein-based NMR screening methodologies for detecting compounds...
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[NMR paper] Rapid screening of E. coli extracts by heteronuclear NMR.
Rapid screening of E. coli extracts by heteronuclear NMR.
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Curr Protoc Protein Sci. 2003 May;Chapter 7:Unit 7.11
Authors: Gronenborn AM
Assessing whether a protein or protein complex is amenable to structural analysis is an important component in the structural genomics effort. In particular, if complete sets of structures for entire genomes are to be obtained within a reasonable time frame, high throughput methodologies for all steps along the way have to be developed....
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[NMR paper] Populating the equilibrium molten globule state of apomyoglobin under conditions suit
Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR.
FEBS Lett. 1997 Nov 3;417(1):92-6
Authors: Eliezer D, Jennings PA, Dyson HJ, Wright PE
Conditions have been determined under which the equilibrium molten globule...
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[NMR paper] Rapid amide proton exchange rates in peptides and proteins measured by solvent quench
Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.
Protein Sci. 1995 Apr;4(4):804-14
Authors: Zhang YZ,...
Microdrop screening: a rapid method to optimize solvent conditions for NMR spectrosco
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