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 relaxation rate ratio R 1/R 2 assumes a single-component tumbling correlation function, and thus can provide incorrect results as soon as the â??long tailâ?? is of relevance. This effect, however, has been underestimated in many instances. In this work we present a detailed systematic study of the tumbling correlation function of two proteins, lysozyme and bovine serum albumin, at different concentrations and temperatures using proton field-cycling relaxometry combined with R 1Ï? and R 2 measurements. Unlike high-field NMR relaxation methods, these techniques enable a detailed study of dynamics on a time scale longer than the normal protein tumbling correlation time and, thus, a reliable estimate of the parameters of the â??long tailâ??. In this work we analyze the concentration dependence of the intensity and correlation time of the slow component and perform simulations of high-field 15N NMR relaxation data demonstrating the importance of taking the â??long tailâ?? in the analysis into account.
[NMR paper] NMR-Detected Brownian Dynamics of ?B-Crystallin over a Wide Range of Concentrations.
NMR-Detected Brownian Dynamics of ?B-Crystallin over a Wide Range of Concentrations.
NMR-Detected Brownian Dynamics of ?B-Crystallin over a Wide Range of Concentrations.
Biophys J. 2015 Jan 6;108(1):98-106
Authors: Roos M, Link S, Balbach J, Krushelnitsky A, Saalwächter K
Abstract
Knowledge about the global translational and rotational motion of proteins under crowded conditions is highly relevant for understanding the function of proteins in*vivo. This holds in particular for human ?B-crystallin, which is strongly crowded...
nmrlearner
Journal club
0
01-08-2015 01:29 PM
Combined zero-quantum and spin-diffusion mixing for efficient homonuclear correlation spectroscopy under fast MAS: broadband recoupling and detection of long-range correlations
Combined zero-quantum and spin-diffusion mixing for efficient homonuclear correlation spectroscopy under fast MAS: broadband recoupling and detection of long-range correlations
Abstract
Fast magic angle spinning (MAS) NMR spectroscopy is emerging as an essential analytical and structural biology technique. Large resolution and sensitivity enhancements observed under fast MAS conditions enable structural and dynamics analysis of challenging systems, such as large macromolecular assemblies and isotopically dilute samples, using only a fraction of...
nmrlearner
Journal club
0
11-25-2014 07:13 AM
[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...
nmrlearner
Journal club
1
06-26-2014 07:13 AM
[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...
nmrlearner
Journal club
0
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...
nmrlearner
Journal club
0
12-21-2013 03:15 PM
[NMR paper] Measurement of long-range cross-correlation rates using a combination of single- and
Measurement of long-range cross-correlation rates using a combination of single- and multiple-quantum NMR spectroscopy in one experiment.
Related Articles Measurement of long-range cross-correlation rates using a combination of single- and multiple-quantum NMR spectroscopy in one experiment.
J Am Chem Soc. 2002 Apr 17;124(15):4050-7
Authors: Fruh D, Chiarparin E, Pelupessy P, Bodenhausen G
A method is described to determine long-range cross-correlations between the modulations of an anisotropic chemical shift (e.g., of a C' carbonyl carbon in...
nmrlearner
Journal club
0
11-24-2010 08:49 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...
nmrlearner
Journal club
0
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
The â??long tailâ?? of the protein tumbling correlation function: observation by 1 H NMR relaxometry in a wide frequency and concentration range
Linear Mode
