Literature DB >> 16199658

Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.

Ronald W Peterson1, Maxim S Pometun, Zhengshuang Shi, A Joshua Wand.   

Abstract

NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids is emerging as a tool for biophysical studies of proteins in atomic detail in a variety of otherwise inaccessible contexts. The central element of the approach is the encapsulation of the protein of interest within the aqueous core of a reverse micelle with high structural fidelity. The process of encapsulation is highly dependent upon the nature of the surfactant(s) employed. Here we describe novel mixtures of surfactants that are capable of successfully encapsulating a range of types of proteins under a variety of conditions.

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Year:  2005        PMID: 16199658      PMCID: PMC2253227          DOI: 10.1110/ps.051535405

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  9 in total

1.  Forced folding and structural analysis of metastable proteins.

Authors:  Ronald W Peterson; Karthik Anbalagan; Cecilia Tommos; A Joshua Wand
Journal:  J Am Chem Soc       Date:  2004-08-11       Impact factor: 15.419

2.  Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation.

Authors:  Charles R Babu; Vincent J Hilser; A Joshua Wand
Journal:  Nat Struct Mol Biol       Date:  2004-02-29       Impact factor: 15.369

3.  NMR spectroscopy of proteins encapsulated in a positively charged surfactant.

Authors:  Brian G Lefebvre; Weixia Liu; Ronald W Peterson; Kathleen G Valentine; A Joshua Wand
Journal:  J Magn Reson       Date:  2005-04-07       Impact factor: 2.229

4.  High-resolution NMR studies of encapsulated proteins in liquid ethane.

Authors:  Ronald W Peterson; Brian G Lefebvre; A Joshua Wand
Journal:  J Am Chem Soc       Date:  2005-07-27       Impact factor: 15.419

5.  High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.

Authors:  A J Wand; M R Ehrhardt; P F Flynn
Journal:  Proc Natl Acad Sci U S A       Date:  1998-12-22       Impact factor: 11.205

6.  Main chain and side chain dynamics of oxidized flavodoxin from Cyanobacterium anabaena.

Authors:  W Liu; P F Flynn; E J Fuentes; J K Kranz; M McCormick; A J Wand
Journal:  Biochemistry       Date:  2001-12-11       Impact factor: 3.162

7.  Recombinant equine cytochrome c in Escherichia coli: high-level expression, characterization, and folding and assembly mutants.

Authors:  Jon N Rumbley; Linh Hoang; S Walter Englander
Journal:  Biochemistry       Date:  2002-11-26       Impact factor: 3.162

8.  Aromatic ring-flipping in supercooled water: implications for NMR-based structural biology of proteins.

Authors:  J J Skalicky; J L Mills; S Sharma; T Szyperski
Journal:  J Am Chem Soc       Date:  2001-01-24       Impact factor: 15.419

9.  Internal dynamics of human ubiquitin revealed by 13C-relaxation studies of randomly fractionally labeled protein.

Authors:  A J Wand; J L Urbauer; R P McEvoy; R J Bieber
Journal:  Biochemistry       Date:  1996-05-14       Impact factor: 3.162

  9 in total
  15 in total

1.  Cold denaturation of encapsulated ubiquitin.

Authors:  Maxim S Pometun; Ronald W Peterson; Charles R Babu; A Joshua Wand
Journal:  J Am Chem Soc       Date:  2006-08-23       Impact factor: 15.419

2.  Performance of cryogenic probes as a function of ionic strength and sample tube geometry.

Authors:  Markus W Voehler; Galen Collier; John K Young; Michael P Stone; Markus W Germann
Journal:  J Magn Reson       Date:  2006-09-01       Impact factor: 2.229

3.  Simulations of the confinement of ubiquitin in self-assembled reverse micelles.

Authors:  Jianhui Tian; Angel E García
Journal:  J Chem Phys       Date:  2011-06-14       Impact factor: 3.488

4.  Protein folding in a reverse micelle environment: the role of confinement and dehydration.

Authors:  Anna Victoria Martinez; Susan C DeSensi; Laura Dominguez; Eva Rivera; John E Straub
Journal:  J Chem Phys       Date:  2011-02-07       Impact factor: 3.488

5.  Defining the Apoptotic Trigger: THE INTERACTION OF CYTOCHROME c AND CARDIOLIPIN.

Authors:  Evan S O'Brien; Nathaniel V Nucci; Brian Fuglestad; Cecilia Tommos; A Joshua Wand
Journal:  J Biol Chem       Date:  2015-10-20       Impact factor: 5.157

6.  Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.

Authors:  Nathaniel V Nucci; Bryan S Marques; Sabrina Bédard; Jakob Dogan; John M Gledhill; Veronica R Moorman; Ronald W Peterson; Kathleen G Valentine; Alison L Wand; A Joshua Wand
Journal:  J Biomol NMR       Date:  2011-07-12       Impact factor: 2.835

7.  Water loading driven size, shape, and composition of cetyltrimethylammonium/hexanol/pentane reverse micelles.

Authors:  Brian Fuglestad; Kushol Gupta; A Joshua Wand; Kim A Sharp
Journal:  J Colloid Interface Sci       Date:  2019-01-06       Impact factor: 8.128

Review 8.  High-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.

Authors:  Nathaniel V Nucci; Kathleen G Valentine; A Joshua Wand
Journal:  J Magn Reson       Date:  2014-04       Impact factor: 2.229

9.  Reverse micelles in integral membrane protein structural biology by solution NMR spectroscopy.

Authors:  Joseph M Kielec; Kathleen G Valentine; Charles R Babu; A Joshua Wand
Journal:  Structure       Date:  2009-03-11       Impact factor: 5.006

10.  Solution NMR and CD spectroscopy of an intrinsically disordered, peripheral membrane protein: evaluation of aqueous and membrane-mimetic solvent conditions for studying the conformational adaptability of the 18.5 kDa isoform of myelin basic protein (MBP).

Authors:  David S Libich; George Harauz
Journal:  Eur Biophys J       Date:  2008-05-01       Impact factor: 1.733

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