[NMR paper] The "long tail" of the protein tumbling correlation function: observation by (1)H NMR relaxometry in a wide frequency and concentration range.
Related ArticlesThe "long tail" of the protein tumbling correlation function: observation by (1)H NMR relaxometry in a wide frequency and concentration range.
J Biomol NMR. 2015 Nov 18;
Authors: Roos M, Hofmann M, Link S, Ott M, Balbach J, Rössler E, Saalwächter K, Krushelnitsky A
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 ("long tail") 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 "long tail" 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 1? 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 "long tail". In this work we analyze the concentration dependence of the intensity and correlation time of the slow component and perform simulations of high-field (15)N NMR relaxation data demonstrating the importance of taking the "long tail" in the analysis into account.
PMID: 26582718 [PubMed - as supplied by publisher]
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
[NMRpipe Yahoo group] Re: Bug in nmrDraw's "2D Limits" function?
Re: Bug in nmrDraw's "2D Limits" function?
Hi ... Sorry, this must be annoying. On my Fedora Core 12 test system, setting the "2D Limits" menu locations to ppm pts or % seems to work ok. But, in my
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[NMRpipe Yahoo group] Bug in nmrDraw's "2D Limits" function?
Bug in nmrDraw's "2D Limits" function?
Hi, I'm using the current version of NMRPipe on linux, and there's a problem in nmrDraw with the "Display Limits" function (Menu Draw > 2D Limits; keyboard
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[NMR paper] Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC
Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments.
Related Articles Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments.
J Am Chem Soc. 2002 Oct 16;124(41):12352-60
Authors: Skrynnikov NR, Dahlquist FW, Kay LE
Carr-Purcell-Meiboom-Gill (CPMG) relaxation measurements employing trains of 180 degrees pulses with variable pulse spacing provide valuable information about systems undergoing millisecond-time-scale chemical exchange. Fits of the CPMG relaxation...
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11-24-2010 08:58 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...
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11-24-2010 08:49 PM
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
A postdoctoral position to study the solution dynamics and structure
of protein kinases is available on a NIH funded project (REF#:
HS-R-6453-10-08-S). Our group is interested in how static and dynamic
changes of protein structure affect the activity of protein kinases.
We combine X-ray crystallography, NMR and ligand binding kinetics with
collaborative molecular dynamic studies (See e.g. ref 1 and 2). Our
research group is located at Stony Brook University in a highly
interactive environment with the New York...
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08-21-2010 05:17 AM
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
A postdoctoral position to study the solution dynamics and structure
of protein kinases is available on a NIH funded project (REF#:
HS-R-6453-10-08-S). Our group is interested in how static and dynamic
changes of protein structure affect the activity of protein kinases.
We combine X-ray crystallography, NMR and ligand binding kinetics with
collaborative molecular dynamic studies (See e.g. ref 1 and 2). Our
research group is located at Stony Brook University in a highly
interactive environment with the New York...