Literature DB >> 9390406

The button test: a small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMR.

S Bagby1, K I Tong, D Liu, J R Alattia, M Ikura.   

Abstract

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.

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Year:  1997        PMID: 9390406     DOI: 10.1023/a:1018359305544

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN: 0925-2738            Impact factor:   2.835


  6 in total

Review 1.  Solubility as a function of protein structure and solvent components.

Authors:  C H Schein
Journal:  Biotechnology (N Y)       Date:  1990-04

2.  Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein.

Authors:  S Bagby; S Kim; E Maldonado; K I Tong; D Reinberg; M Ikura
Journal:  Cell       Date:  1995-09-08       Impact factor: 41.582

3.  Discovering high-affinity ligands for proteins: SAR by NMR.

Authors:  S B Shuker; P J Hajduk; R P Meadows; S W Fesik
Journal:  Science       Date:  1996-11-29       Impact factor: 47.728

Review 4.  Prospects for NMR of large proteins.

Authors:  G Wagner
Journal:  J Biomol NMR       Date:  1993-07       Impact factor: 2.835

5.  Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.

Authors:  D S Garrett; Y J Seok; D I Liao; A Peterkofsky; A M Gronenborn; G M Clore
Journal:  Biochemistry       Date:  1997-03-04       Impact factor: 3.162

6.  Characterization of NADP+ binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift changes.

Authors:  K L Constantine; L Mueller; V Goldfarb; M Wittekind; W J Metzler; J Yanchunas; J G Robertson; M F Malley; M S Friedrichs; B T Farmer
Journal:  J Mol Biol       Date:  1997-04-18       Impact factor: 5.469

  6 in total
  14 in total

1.  A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins.

Authors:  P Zhou; A A Lugovskoy; G Wagner
Journal:  J Biomol NMR       Date:  2001-05       Impact factor: 2.835

2.  Expression screening, protein purification and NMR analysis of human protein domains for structural genomics.

Authors:  G E Folkers; B N M van Buuren; R Kaptein
Journal:  J Struct Funct Genomics       Date:  2004

3.  A straight-forward method of optimising protein solubility for NMR.

Authors:  Peter W A Howe
Journal:  J Biomol NMR       Date:  2004-11       Impact factor: 2.835

4.  A method for efficient isotopic labeling of recombinant proteins.

Authors:  J Marley; M Lu; C Bracken
Journal:  J Biomol NMR       Date:  2001-05       Impact factor: 2.835

5.  High-throughput screening of optimal solution conditions for structural biological studies by fluorescence correlation spectroscopy.

Authors:  Toshihiko Sugiki; Chie Yoshiura; Yutaka Kofuku; Takumi Ueda; Ichio Shimada; Hideo Takahashi
Journal:  Protein Sci       Date:  2009-05       Impact factor: 6.725

6.  Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method.

Authors:  Yoshihiro Kobashigawa; Hiroyuki Kumeta; Kenji Ogura; Fuyuhiko Inagaki
Journal:  J Biomol NMR       Date:  2009-01-13       Impact factor: 2.835

Review 7.  Solution NMR structure determination of proteins revisited.

Authors:  Martin Billeter; Gerhard Wagner; Kurt Wüthrich
Journal:  J Biomol NMR       Date:  2008-10-01       Impact factor: 2.835

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

Authors:  C A Lepre; J M Moore
Journal:  J Biomol NMR       Date:  1998-11       Impact factor: 2.835

9.  1H, 15N, and 13C NMR resonance assignments for the Eps15 homology domain of Reps1.

Authors:  S Kim; A M Dubelman; S Goonesekera; L A Feig; J D Baleja
Journal:  J Biomol NMR       Date:  2000-12       Impact factor: 2.835

10.  Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies.

Authors:  Pei Zhou; Gerhard Wagner
Journal:  J Biomol NMR       Date:  2010-01       Impact factor: 2.835

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