The abundances of 31 major proteins in human plasma, measured by selected reaction monitoring mass spectrometry, remained remarkably steady over 4 months, strengthening their case to be used as disease biomarkers.
Improving protein solubility & long-term stability
Has anybody successfully used the following method?
A simple method for improving protein solubility and long-term stability.
Golovanov AP, Hautbergue GM, Wilson SA, Lian LY.
Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, P. O. Box 88, Manchester M60 1QD, UK. a.golovanov@umist.ac.jp
J Am Chem Soc. 2004 Jul 28;126(29):8933-9.
nmrlearner
Proteins
4
01-22-2014 07:04 PM
[Question from NMRWiki Q&A forum] How long is too long a pulse?
How long is too long a pulse?
I recently calibrated the 90 for 11B on a Agilent 400MR. The 1H 90 was about 6.8us at 59dB... It turns out to be 22.6us for 11B at 59dB. Is this long enough that I should consider upping the pulse power?
More generally, how long is too long a pulse in general?
Check if somebody has answered this question on NMRWiki QA forum
nmrlearner
News from other NMR forums
0
07-16-2012 06:33 PM
[Question from NMRWiki Q&A forum] What will happen if I use long pulse?
What will happen if I use long pulse?
Hello everybody. We have an AVANCE 500 MHz bruker instrument. Unfortunately, our amplifier has been weakened and I can not reach 90 degree pulse for X nuclei channel. When I increase the power (decrease the Pl in XWin NMR) my signal always grow. I am going to use long pulses with duration of 80 microsecond to 100 microsecond or even more to reach 90 degree pulse instead of common pulses which are about 10 microsecond. Is this situation hurt any part of instrument? Or I only lose current broad excitation band and will be forced to take several spectrum...
nmrlearner
News from other NMR forums
0
07-06-2012 05:21 PM
[NMR900 blog] "Anarchy in the proteome" - interview with Julie Forman-Kay
"Anarchy in the proteome" - interview with Julie Forman-Kay
Julie Forman-Kay (Toronto) speaks about her research in disordered proteins in a podcast interview to the Chemistry World. Available for download at
Chemistry World Podcast, August 2011, "6.05-13.00 Julie Forman-Kay reveals that disordered, unfolded proteins are much more functional and much more common than previously thought"
http://www.rsc.org/chemistryworld/podcast/CWpodcast.asp
Part of this interview is also featured in the printed August 2011 issue of the Chemistry World (subscription required): M. Gross "Anarchy in...
nmrlearner
News from NMR blogs
0
08-04-2011 01:14 AM
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
J Biol Chem. 2011 May 3;
Authors: Shin J, Chakraborty G, Bharatham N, Kang C, Tochio N, Koshiba S, Kigawa T, Kim W, Kim KT, Yoon HS
Vaccinia-related kinase 1 (VRK1) is one of the mitotic kinases which play important roles in cell cycle, nuclear condensation and transcription regulation. Kinase...
nmrlearner
Journal club
0
05-06-2011 12:02 PM
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
J Phys Chem B. 2011 Feb 10;
Authors: Bertelsen K, Vad B, Nielsen EH, Hansen SK, Skrydstrup T, Otzen DE, Vosegaard T, Nielsen NC
Recently, ether lipids have been introduced as long-term stable alternatives to the more natural,...
nmrlearner
Journal club
0
02-12-2011 05:26 PM
[NMR paper] Influence of pH on NMR structure and stability of the human prion protein globular do
Influence of pH on NMR structure and stability of the human prion protein globular domain.
Related Articles Influence of pH on NMR structure and stability of the human prion protein globular domain.
J Biol Chem. 2003 Sep 12;278(37):35592-6
Authors: Calzolai L, Zahn R
The NMR structure of the globular domain of the human prion protein (hPrP) with residues 121-230 at pH 7.0 shows the same global fold as the previously published structure determined at pH 4.5. It contains three alpha-helices, comprising residues 144-156, 174-194, and 200-228, and...
Long-term stability of human proteome
The abundances of 31 major proteins in human plasma, measured by selected reaction monitoring mass spectrometry, remained remarkably steady over 4 months, strengthening their case to be used as disease biomarkers.
Linear Mode
