Microdrop screening: a rapid method to optimize solvent conditions for NMR spectroscopy of proteins

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 mi...

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Bibliographic Details
Published in:Journal of biomolecular NMR 1998-11, Vol.12 (4), p.493-499
Main Authors: Lepre, C A, Moore, J M
Format: Article
Language:English
Subjects:
Buffers
Glia Maturation Factor
Humans
Nerve Growth Factors - chemistry
Nerve Tissue Proteins - chemistry
Nuclear Magnetic Resonance, Biomolecular - methods
Protein Conformation
Protein folding
Proteins - chemistry
Recombinant Proteins - chemistry
Solvents
Spectrum analysis
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Summary: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.
ISSN:0925-2738
1573-5001
DOI:10.1023/a:1008353000679