The â??long tailâ?? of the protein tumbling correlation function: observation by 1 H NMR relaxometry in a wide frequency and concentration range
The â??long tailâ?? of the protein tumbling correlation function: observation by 1 H NMR relaxometry in a wide frequency and concentration range
Abstract
Inter-protein interactions in solution affect the auto-correlation function of Brownian tumbling not only in terms of a simple increase of the correlation time, they also lead to the appearance of a weak slow component (â??long tailâ??) of the correlation function due to a slowly changing local anisotropy of the microenvironment. The conventional protocol of correlation time estimation from the...
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11-19-2015 05:22 PM
[NMR paper] Long-range effects of tag sequence on marginally stabilized structure in HIV-1 p24 capsid protein monitored using NMR.
Long-range effects of tag sequence on marginally stabilized structure in HIV-1 p24 capsid protein monitored using NMR.
Long-range effects of tag sequence on marginally stabilized structure in HIV-1 p24 capsid protein monitored using NMR.
Biochim Biophys Acta. 2014 Jun 21;
Authors: Okazaki H, Kaneko C, Hirahara M, Watanabe S, Tochio N, Kigawa T, Nishimura C
Abstract
N-terminal domain of HIV-1 p24 capsid protein is a globular fold composed of seven helices and two ?-strands with a flexible structure including the ?4-5 loop and...
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06-26-2014 07:13 AM
Long-range effects of tag sequence on marginally stabilized structure in HIV-1 p24 capsid protein monitored using NMR
Long-range effects of tag sequence on marginally stabilized structure in HIV-1 p24 capsid protein monitored using NMR
Publication date: Available online 21 June 2014
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics</br>
Author(s): Honoka Okazaki , Chie Kaneko , Miyuki Hirahara , Satoru Watanabe , Naoya Tochio , Takanori Kigawa , Chiaki Nishimura</br>
N-terminal domain of HIV-1 p24 capsid protein is a globular fold composed of seven helices and two ?-strands with a flexible structure including the ?4-5 loop and both N- and C-terminal ends....
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06-21-2014 10:12 PM
[NMR paper] Structure determination of protein-protein complexes with long-range anisotropic paramagnetic NMR restraints.
Structure determination of protein-protein complexes with long-range anisotropic paramagnetic NMR restraints.
Related Articles Structure determination of protein-protein complexes with long-range anisotropic paramagnetic NMR restraints.
Curr Opin Struct Biol. 2014 Feb;24C:45-53
Authors: Hass MA, Ubbink M
Abstract
Paramagnetic NMR spectroscopy has evolved rapidly in the last decade, and has shown to be a very useful tool for solving structures of protein-protein complexes. A major breakthrough has been the development of...
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04-12-2014 06:36 PM
Structure determination of protein–protein complexes with long-range anisotropic paramagnetic NMR restraints
Structure determination of protein–protein complexes with long-range anisotropic paramagnetic NMR restraints
Publication date: February 2014
Source:Current Opinion in Structural Biology, Volume 24</br>
Author(s): Mathias AS Hass , Marcellus Ubbink</br>
Paramagnetic NMR spectroscopy has evolved rapidly in the last decade, and has shown to be a very useful tool for solving structures of protein–protein complexes. A major breakthrough has been the development of paramagnetic metal binding tags that can be attached specifically to the protein. These tags have greatly...
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12-21-2013 03:15 PM
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
Rasmus Linser, Benjamin Bardiaux, Victoria Higman, Uwe Fink and Bernd Reif
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja110222h/aop/images/medium/ja-2010-10222h_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja110222h
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Dh0EBf8PwcY
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03-24-2011 08:02 PM
[NMR paper] De novo determination of protein structure by NMR using orientational and long-range
De novo determination of protein structure by NMR using orientational and long-range order restraints.
Related Articles De novo determination of protein structure by NMR using orientational and long-range order restraints.
J Mol Biol. 2000 May 19;298(5):927-36
Authors: Hus JC, Marion D, Blackledge M
Orientational and novel long-range order restraints available from paramagnetic systems have been used to determine the backbone solution structure of the cytochrome c' protein to atomic resolution in the complete absence of restraints derived from...
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11-18-2010 09:15 PM
Antifreeze Glycoprotein Activity Correlates with Long-Range Protein-Water Dynamics
Antifreeze Glycoprotein Activity Correlates with Long-Range Protein-Water Dynamics
Simon Ebbinghaus et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1051632/aop/images/medium/ja-2010-051632_0004.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society