Related ArticlesThe button test: a small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMR.
J Biomol NMR. 1997 Oct;10(3):279-82
Authors: Bagby S, Tong KI, Liu D, Alattia JR, Ikura M
A simple method has been developed for screening solution conditions to determine conditions under which a protein is soluble at the high concentrations typically used for NMR spectroscopy. The method employs microdialysis cells or 'buttons'. The low sample volume (5 microliters) required for each microdialysis button permits testing of a wide range of solution conditions and temperatures with high protein concentrations, using a small amount of protein. Following precipitation of several NMR samples of the C-terminal core domain of human TFIIB, the microdialysis button screen facilitated identification of conditions in which precipitation of the TFIIB core domain was eliminated. The microdialysis button method for screening solution conditions is generally applicable and has been used to permit rapid identification of suitable NMR sample solution conditions for proteins involved in transcription and cell adhesion.
[NMR paper] Multidimensional NMR spectroscopy for protein characterization and assignment inside cells.
Multidimensional NMR spectroscopy for protein characterization and assignment inside cells.
Related Articles Multidimensional NMR spectroscopy for protein characterization and assignment inside cells.
J Am Chem Soc. 2005 Aug 10;127(31):10848-9
Authors: Reardon PN, Spicer LD
High-field, heteronuclear NMR spectroscopy of biological macromolecules in native cellular environments is limited by the low concentrations present and the long data acquisition times needed for the experiments. Successful 1D and 2D heteronuclear NMR data have been...
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[NMR paper] Assessing precision and accuracy of protein structures derived from NMR data.
Assessing precision and accuracy of protein structures derived from NMR data.
Related Articles Assessing precision and accuracy of protein structures derived from NMR data.
Proteins. 2005 Jun 1;59(4):655-61
Authors: Snyder DA, Bhattacharya A, Huang YJ, Montelione GT
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[NMR paper] Application of sparse NMR restraints to large-scale protein structure prediction.
Application of sparse NMR restraints to large-scale protein structure prediction.
Related Articles Application of sparse NMR restraints to large-scale protein structure prediction.
Biophys J. 2004 Aug;87(2):1241-8
Authors: Li W, Zhang Y, Skolnick J
The protein structure prediction algorithm TOUCHSTONEX that uses sparse distance restraints derived from NMR nuclear Overhauser enhancement (NOE) data to predict protein structures at low-to-medium resolution was evaluated as follows: First, a representative benchmark set of the Protein Data Bank...
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[NMR paper] Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N r
Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
Related Articles Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
J Am Chem Soc. 2001 Feb 7;123(5):967-75
Authors: Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE
A new NMR experiment is presented for...
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[NMR paper] Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-
Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.
Related Articles Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.
J Biomol Struct Dyn. 1999 Aug;17(1):157-74
Authors: Orekhov VY, Korzhnev DM, Pervushin KV, Hoffmann E, Arseniev AS
This paper presents a procedure for detection of intermediate nanosecond internal dynamics in globular proteins. The procedure uses 1H-15N relaxation measurements at several spectrometer frequencies...
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[NMR images] 1D spectrum of a small protein
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1D spectrum of a small protein
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Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Si
Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Site-Specific NMR Relaxation Rates.
Related Articles Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Site-Specific NMR Relaxation Rates.
J Am Chem Soc. 2010 Aug 6;
Authors: Krushelnitsky A, Zinkevich T, Reichert D, Chevelkov V, Reif B
For the first time, we have demonstrated the site-resolved measurement of reliable (i.e., free of interfering effects) (15)N R(1rho) relaxation rates from a solid protein to extract dynamic...
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Assessing precision and accuracy of protein struct
Editor's Corner
Assessing precision and accuracy of protein structures derived from NMR data
David A. Snyder 1 2, Aneerban Bhattacharya 1 2, Yuanpeng J. Huang 1 2, Gaetano T. Montelione 1 2 *
1Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, and Northeast Structural Genomics Consortium, Rutgers University, Piscataway, NJ 08854
2Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Piscataway, NJ 08854
*Correspondence to Gaetano T. Montelione, CABM-Rutgers University, 679 Hoes Lane, Piscataway, NJ...
The button test: a small scale method using microdialysis cells for assessing protein
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