Literature DB >> 16508692

Self contained high pressure cell, apparatus and procedure for the preparation of encapsulated proteins dissolved in low viscosity fluids for NMR spectroscopy.

Ronald W Peterson1, A Joshua Wand.   

Abstract

The design of a sample cell for high performance nuclear magnetic resonance (NMR) at elevated pressure is described. The cell has been optimized for the study of encapsulated proteins dissolved in low viscosity fluids but is suitable for more general NMR spectroscopy of biomolecules at elevated pressure. The NMR cell is comprised of an alumina toughened zirconia tube mounted on a self-sealing non-magnetic metallic valve. The cell has several advantages including relatively low cost, excellent NMR performance, high pressure tolerance, chemical inertness and a relatively large active volume. Also described is a low volume sample preparation device which allows for the preparation of samples under high hydrostatic pressure and their subsequent transfer to the NMR cell.

Entities:  

Year:  2005        PMID: 16508692      PMCID: PMC1343520          DOI: 10.1063/1.2038087

Source DB:  PubMed          Journal:  Rev Sci Instrum        ISSN: 0034-6748            Impact factor:   1.523


  14 in total

1.  Preparation of encapsulated proteins dissolved in low viscosity fluids.

Authors:  M R Ehrhardt; P F Flynn; A J Wand
Journal:  J Biomol NMR       Date:  1999-05       Impact factor: 2.835

Review 2.  On-line cell high-pressure nuclear magnetic resonance technique: application to protein studies.

Authors:  K Akasaka; H Yamada
Journal:  Methods Enzymol       Date:  2001       Impact factor: 1.600

Review 3.  High-resolution nuclear magnetic resonance studies of proteins.

Authors:  Jiri Jonas
Journal:  Biochim Biophys Acta       Date:  2002-03-25

4.  A simple and effective NMR cell for studies of encapsulated proteins dissolved in low viscosity solvents.

Authors:  Peter F Flynn; Mark J Milton; Charles R Babu; A Joshua Wand
Journal:  J Biomol NMR       Date:  2002-08       Impact factor: 2.835

Review 5.  High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins.

Authors:  Yuji O Kamatari; Ryo Kitahara; Hiroyuki Yamada; Shigeyuki Yokoyama; Kazuyuki Akasaka
Journal:  Methods       Date:  2004-09       Impact factor: 3.608

6.  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

7.  Hydrostatic and osmotic pressure as tools to study macromolecular recognition.

Authors:  C R Robinson; S G Sligar
Journal:  Methods Enzymol       Date:  1995       Impact factor: 1.600

8.  Pressure-induced reversible dissociation of enolase.

Authors:  A A Paladini; G Weber
Journal:  Biochemistry       Date:  1981-04-28       Impact factor: 3.162

9.  Dissection of the pathway of molecular recognition by calmodulin.

Authors:  James K Kranz; Peter F Flynn; Ernesto J Fuentes; A Joshua Wand
Journal:  Biochemistry       Date:  2002-02-26       Impact factor: 3.162

10.  The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.

Authors:  M W Lassalle; H Yamada; K Akasaka
Journal:  J Mol Biol       Date:  2000-04-28       Impact factor: 5.469

View more
  26 in total

1.  Importance of time-ordered non-uniform sampling of multi-dimensional NMR spectra of Aβ1-42 peptide under aggregating conditions.

Authors:  Jinfa Ying; C Ashley Barnes; John M Louis; Ad Bax
Journal:  J Biomol NMR       Date:  2019-08-12       Impact factor: 2.835

2.  High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape.

Authors:  Martin J Fossat; Thuy P Dao; Kelly Jenkins; Mariano Dellarole; Yinshan Yang; Scott A McCallum; Angel E Garcia; Doug Barrick; Christian Roumestand; Catherine A Royer
Journal:  Biophys J       Date:  2016-12-06       Impact factor: 4.033

Review 3.  Lessons from pressure denaturation of proteins.

Authors:  Julien Roche; Catherine A Royer
Journal:  J R Soc Interface       Date:  2018-10-03       Impact factor: 4.118

4.  Pressure dependence of side chain 13C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH2.

Authors:  Markus Beck Erlach; Joerg Koehler; Edson Crusca; Claudia E Munte; Masatsune Kainosho; Werner Kremer; Hans Robert Kalbitzer
Journal:  J Biomol NMR       Date:  2017-09-14       Impact factor: 2.835

5.  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

6.  What makes proteins work: exploring life in P-T-X.

Authors:  Toshiko Ichiye
Journal:  Phys Biol       Date:  2016-11-15       Impact factor: 2.583

7.  Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR.

Authors:  Cyril Charlier; Joseph M Courtney; T Reid Alderson; Philip Anfinrud; Ad Bax
Journal:  J Am Chem Soc       Date:  2018-06-25       Impact factor: 15.419

8.  Solution NMR investigation of the response of the lactose repressor core domain dimer to hydrostatic pressure.

Authors:  Brian Fuglestad; Matthew A Stetz; Zachary Belnavis; A Joshua Wand
Journal:  Biophys Chem       Date:  2017-02-24       Impact factor: 2.352

9.  Reverse Micelle Encapsulation of Proteins for NMR Spectroscopy.

Authors:  Brian Fuglestad; Bryan S Marques; Christine Jorge; Nicole E Kerstetter; Kathleen G Valentine; A Joshua Wand
Journal:  Methods Enzymol       Date:  2018-12-10       Impact factor: 1.600

Review 10.  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

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.