Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell [Biophysics and Computational Biology]
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell
Cyril Charlier, T. Reid Alderson, Joseph M. Courtney, Jinfa Ying, Philip Anfinrud, Adriaan Bax...
Date: 2018-05-01
In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded and unfolded states, their thermodynamic equilibrium can be altered by varying the hydrostatic pressure. Using a pressure-sensitized mutant of ubiquitin, we demonstrate that rapidly switching the...
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05-01-2018 10:57 PM
[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] The Structure of Mouse Cytomegalovirus m04 Protein Obtained from Sparse NMR Data Reveals a Conserved Fold of the m02-m06 Viral Immune Modulator Family.
The Structure of Mouse Cytomegalovirus m04 Protein Obtained from Sparse NMR Data Reveals a Conserved Fold of the m02-m06 Viral Immune Modulator Family.
Related Articles The Structure of Mouse Cytomegalovirus m04 Protein Obtained from Sparse NMR Data Reveals a Conserved Fold of the m02-m06 Viral Immune Modulator Family.
Structure. 2014 Aug 6;
Authors: Sgourakis NG, Natarajan K, Ying J, Vogeli B, Boyd LF, Margulies DH, Bax A
Abstract
Immunoevasins are key proteins used by viruses to subvert host immune responses. Determining their...
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08-16-2014 10:26 PM
The Structure of Mouse Cytomegalovirus m04 Protein Obtained from Sparse NMR Data Reveals a Conserved Fold of the m02-m06 Viral Immune Modulator Family
The Structure of Mouse Cytomegalovirus m04 Protein Obtained from Sparse NMR Data Reveals a Conserved Fold of the m02-m06 Viral Immune Modulator Family
Publication date: Available online 7 August 2014
Source:Structure</br>
Author(s): Nikolaos*G. Sgourakis , Kannan Natarajan , Jinfa Ying , Beat Vogeli , Lisa*F. Boyd , David*H. Margulies , Ad Bax</br>
Immunoevasins are key proteins used by viruses to subvert host immune responses. Determining their high-resolution structures is key to understanding virus-host interactions toward the design of vaccines and other...
Study reveals evolutionary origins of fold-switching protein - pnas.org
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