Related ArticlesOvercoming solvent saturation-transfer artifacts in protein NMR at neutral pH. Application of pulsed field gradients in measurements of 1H-15N Overhauser effects.
J Magn Reson B. 1994 Sep;105(1):45-51
Authors: Li YC, Montelione GT
Artifacts due to solvent saturation-transfer effects result in incorrect measurements of 1H-15N heteronuclear NOE (HNOE). These artifacts are commonly observed in aqueous protein solutions at neutral pH. We describe the application of pulsed field gradients (PFGs) together with long recycle delays in overcoming errors in HNOE measurements which arise from H2O solvent preirradiation and solvent saturation transfer. Even in the absence of explicit solvent irradiation, the HNOE pulse sequence itself results in a nonequilibrium spin-state distribution of solvent nuclei which can then be transferred by chemical exchange into amide-proton sites. This effect can be avoided by using PFGs for suppression of solvent H2O together with a recycle delay sufficiently long for the magnetization of water to relax back to equilibrium values during the preparation period. These effects were studied in 15N-enriched human type alpha transforming growth factor at pH 7.1. Comparisons of PFG-HNOE experiments with and without selective H2O irradiation and with different recycle times provide estimates of the effects of solvent irradiation on HNOE measurements, which are different for different amide nitrogen-15 nuclei. The amplitudes of these artificial HNOE enhancements are roughly correlated with solvent accessibilities of amide sites in the three-dimensional structure of hTGF alpha.
[Question from NMRWiki Q&A forum] Can anyone help me with Saturation Transfer NMR
Can anyone help me with Saturation Transfer NMR
Hi I am working on a Varian 500MHz NMR. I am attempting to use the pulse sequence satxfer1D to measure the rate constant of an exchanging system. I am not using solvent suppression and I am having trouble understanding the physics behind the "mixing time" after the 90 pulse. I also do not know how many iterations the selective pulse should go through because it seems that if I turn the mixing time off and just use a selective pulse, and then a pw90, I will still obtain the same spectrum no matter how many iterations the selective pulse train...
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09-29-2011 07:36 PM
[U. of Ottawa NMR Facility Blog] Saturation Transfer and Exchange
Saturation Transfer and Exchange
Exchange processes that occur on the NMR time scale affect the NMR line shapes and can be studied by line shape analysis. If the exchange process is slow on the NMR time scale, one can employ EXSY or inversion transfer methods to study the exchange. An alternative to these is the saturation transfer technique. In this method, one of the slowly exchanging resonances (A) is saturated with low power CW irradiation and the effect on the intensity of the resonance of the exchange partner (B) is monitored. If there is exchange between A and B during the period of...
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08-03-2011 01:00 AM
[NMR paper] Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Related Articles Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
J Am Chem Soc. 2005 Sep 28;127(38):13110-1
Authors: Soubias O, Gawrisch K
We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR). The results indicate a strong preference for interaction of rhodopsin with the...
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12-01-2010 06:56 PM
[NMR paper] SOS-NMR: a saturation transfer NMR-based method for determining the structures of pro
SOS-NMR: a saturation transfer NMR-based method for determining the structures of protein-ligand complexes.
Related Articles SOS-NMR: a saturation transfer NMR-based method for determining the structures of protein-ligand complexes.
J Am Chem Soc. 2004 Mar 3;126(8):2390-8
Authors: Hajduk PJ, Mack JC, Olejniczak ET, Park C, Dandliker PJ, Beutel BA
An NMR-based alternative to traditional X-ray crystallography and NMR methods for structure-based drug design is described that enables the structure determination of ligands complexed to virtually...
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11-24-2010 09:25 PM
Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed int
Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed integrin αvβ6 protein-peptide interactions.
Related Articles Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed integrin αvβ6 protein-peptide interactions.
Chem Commun (Camb). 2010 Sep 13;
Authors: Wagstaff JL, Vallath S, Marshall JF, Williamson RA, Howard MJ
We report the first example of peptide-protein heteronuclear two-dimensional (2D) saturation transfer difference nuclear magnetic resonance (STD NMR). This method, resulting in...
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09-15-2010 02:26 PM
[Question from NMRWiki Q&A forum] saturation transfer method in NMR
saturation transfer method in NMR
What is meant by saturation transfer method in NMR? How it is useful in giving the structure of blue copper proteins like Azurin, Plastocyanin and Stellacyani? What is the need to go for this technique in blue copper proteins?
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08-27-2010 07:58 PM
[NMR paper] 31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenin
31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenine nucleotide translocase.
Related Articles 31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenine nucleotide translocase.
Biochemistry. 1991 Aug 27;30(34):8351-7
Authors: Masiakos PT, Williams GD, Berkich DA, Smith MB, LaNoue KF
The exchange of intramitochondrial ATP (ATP(in)) for extramitochondrial ATP (ATP(out)) was measured by using 31P NMR spectroscopy over a range of temperatures in isolated rat liver mitochondria oxidizing...
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08-21-2010 11:12 PM
[NMR paper] 31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenin
31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenine nucleotide translocase.
Related Articles 31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenine nucleotide translocase.
Biochemistry. 1991 Aug 27;30(34):8351-7
Authors: Masiakos PT, Williams GD, Berkich DA, Smith MB, LaNoue KF
The exchange of intramitochondrial ATP (ATP(in)) for extramitochondrial ATP (ATP(out)) was measured by using 31P NMR spectroscopy over a range of temperatures in isolated rat liver mitochondria oxidizing...
Overcoming solvent saturation-transfer artifacts in protein NMR at neutral pH. Applic
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