[NMR paper] Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
Related Articles Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
Proc Natl Acad Sci U S A. 2018 Apr 16;:
Authors: Charlier C, Alderson TR, Courtney JM, Ying J, Anfinrud P, Bax A
Abstract
In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded...
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04-19-2018 01:52 PM
[NMR paper] Solution NMR investigation of the response of the lactose repressor core domain dimer to hydrostatic pressure.
Solution NMR investigation of the response of the lactose repressor core domain dimer to hydrostatic pressure.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution NMR investigation of the response of the lactose repressor core domain dimer to hydrostatic pressure.
Biophys Chem. 2017 Feb 24;:
Authors: Fuglestad B, Stetz MA, Belnavis Z, Joshua Wand A
Abstract
Previous investigations of the sensitivity of the lac repressor to...
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03-03-2017 10:56 PM
[NMR paper] Kinase in Motion: Insights into the Dynamic Nature of p38? by High-Pressure NMR Spectroscopic Studies.
Kinase in Motion: Insights into the Dynamic Nature of p38? by High-Pressure NMR Spectroscopic Studies.
Kinase in Motion: Insights into the Dynamic Nature of p38? by High-Pressure NMR Spectroscopic Studies.
Chembiochem. 2013 Jul 10;
Authors: Nielsen G, Jonker HR, Vajpai N, Grzesiek S, Schwalbe H
Abstract
Protein kinases are highly dynamic and complex molecules. Here we present high-pressure and relaxation studies of the activated p38? mitogen-activated protein kinase (MAPK). p38? plays a central role in inflammatory diseases such as...
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07-12-2013 06:01 PM
[NMR paper] Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Related Articles Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Chembiochem. 2013 Jun 28;
Authors: Roche J, Ying J, Maltsev AS, Bax A
Abstract
The impact of pressure on the backbone (15) N, (1) H and (13) C chemical shifts in N-terminally acetylated ?-synuclein has been evaluated over a pressure range 1-2500 bar. Even while the chemical shifts fall very close...
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07-03-2013 01:46 PM
[NMR paper] Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.
Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.
Related Articles Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.
Protein Eng Des Sel. 2013 Mar 22;
Authors: Ogura K, Kobashigawa Y, Saio T, Kumeta H, Torikai S, Inagaki F
Abstract
Recently, the hydrostatic pressure refolding method was reported as a practical tool for solubilizing and refolding proteins from inclusion bodies; however, there have been...
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03-26-2013 01:30 PM
[NMR paper] De novo folding of membrane proteins: an exploration of the structure and NMR propert
De novo folding of membrane proteins: an exploration of the structure and NMR properties of the fd coat protein.
Related Articles De novo folding of membrane proteins: an exploration of the structure and NMR properties of the fd coat protein.
J Mol Biol. 2004 Mar 26;337(3):513-9
Authors: Im W, Brooks CL
De novo folding simulations of the major pVIII coat protein from filamentous fd bacteriophage, using a newly developed implicit membrane generalized Born model and replica-exchange molecular dynamics, are presented and discussed. The quality of...
Exploration of the dynamic interplay between lipids and membrane proteins by hydrostatic pressure - Nature.com
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