I am studying the protein backbone dynamics using the standard set of NMR relaxation parameters (R1, R2, NOE). I would like to be sure that there is no aggregation in the sample, and I have doubts about it so far. The best evidence I have is that overall rotational correlation time TAUc, predicted by HYDRONMR, matches exactly the one calculated from averaged R2/R1 values. Can anyone tell me for sure it is enough and I can be sure that protein doesn't form dimers/oligomers?
Thanks!
Check if somebody has answered this question on NMRWiki QA forum
Did you find this post helpful? |
Similar Threads
Thread
Thread Starter
Forum
Replies
Last Post
[NMRpipe Yahoo group] Correct for a shifting lock
Correct for a shifting lock
Hello all, In some interleaved relaxation experiments, we've noticed that one of our spectrometers is having trouble locking and the signals (FIDs) shift ever
More...
NMRpipe Yahoo group news
News from other NMR forums
0
02-06-2012 03:54 PM
[NMRpipe Yahoo group] Correct for a shifting lock
Correct for a shifting lock
Hello all, In some interleaved relaxation experiments, we've noticed that one of our spectrometers is having trouble locking and the signals (FIDs) shift ever
More...
NMRpipe Yahoo group news
News from other NMR forums
0
01-13-2012 11:04 PM
[NMR paper] Spectroscopic characterization of nanoErythrosomes in the absence and presence of con
Spectroscopic characterization of nanoErythrosomes in the absence and presence of conjugated polyethyleneglycols: an FTIR and (31)P-NMR study.
Related Articles Spectroscopic characterization of nanoErythrosomes in the absence and presence of conjugated polyethyleneglycols: an FTIR and (31)P-NMR study.
Biochim Biophys Acta. 2002 Aug 31;1564(2):317-24
Authors: Pouliot R, Saint-Laurent A, Chypre C, Audet R, Vitté-Mony I, -Gaudreault RC, Auger M
We have recently developed from red blood cells a new delivery system called nanoErythrosomes. These...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] NMR evidence for progressive stabilization of native-like structure upon aggregation
NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN.
Related Articles NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN.
J Mol Biol. 2000 Jan 14;295(2):239-55
Authors: Alexandrescu AT, Lamour FP, Jaravine VA
The acid-denatured form of the protein LysN aggregates reversibly at pH 2.0. The strength of self-association increases with increasing Cl(-) anion concentration. At low concentrations of protein or Cl(-) anion, resonances of...
nmrlearner
Journal club
0
11-18-2010 09:15 PM
[NMR paper] Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxy
Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxylase: an NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxylase: an NMR study.
Biochemistry. 1997 Dec 2;36(48):14676-82
Authors: Reddy DV, Shenoy BC, Carey PR, Sönnichsen FD
Transcarboxylase (TC) is a biotin-containing enzyme catalyzing the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form...
nmrlearner
Journal club
0
08-22-2010 05:08 PM
[NMR software blog] Can Zero-Filling Correct the Baseline?
Can Zero-Filling Correct the Baseline?
I want to show you a proton spectrum that has puzzled me during the last weeks. It contains something that's quite typical and something that I can't explain. I have processed the spectrum in two different ways, with zero-filling and without it. The spectrum without zero-filling is black, the spectrum with zero-filling is green (the number of points is doubled).
http://2.bp.blogspot.com/_ROkYShLRKqA/TGu61b5bG7I/AAAAAAAAAUQ/9AbsXlWbKUY/s400/TMS.pngThis detail is the bottom part of the TMS signal (magnified to show the ringing effect). Where does the...
nmrlearner
News from NMR blogs
0
08-21-2010 06:29 PM
Correct mis-referenced NMR shifts with MANI-LACS
MANI-LACS Server v. 0.1 (Beta)
MANI-LACS offers a new approach to NMR reference correction and outlier identification that achieves excellent results using only residue specific chemical shift assignment.
http://bija.nmrfam.wisc.edu/MANI-LACS/seeds.jpg
Instructions for preparing input files
Database of chemical shift corrections
nmrlearner
General
0
08-14-2005 09:11 PM
New way to correct misreferenced chemical shifts
A simple method to adjust inconsistently referenced 13C and 15N chemical shift assignments of proteins.
Wang Y, Wishart DS.
J Biomol NMR. 2005 Feb;31(2):143-8.
http://pronmr.com/yunjunwang_files/yjw_pssi.jpg
Abstract: