The pressure dependence of the one-bond indirect spinâ??spin coupling constants 1 JNâ??H was studied in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (with Xxx being one of the 20 proteinogenic amino acids). The response of the 1 JNâ??H coupling constants is amino acid type specific, with an average increase of its magnitude by 0.6Â*Hz at 200Â*MPa. The variance of the pressure response is rather large, the largest pressure effect is observed for asparagine where the coupling constant becomes more negative by â??2.9Â*Hz at 200Â*MPa. The size of the J-coupling constant at high pressure is positively correlated with its low pressure value and the β-propensity, and negatively correlated with the amide proton shift and the first order nitrogen pressure coefficient and the electrostatic solvation free energy.
[NMR paper] Detection of a transient intramolecular hydrogen bond using 1JNH scalar couplings
Detection of a transient intramolecular hydrogen bond using 1JNH scalar couplings
Publication date: Available online 18 April 2014
Source:Journal of Magnetic Resonance</br>
Author(s): ShengQi Xiang , Markus Zweckstetter</br>
Hydrogen bonds are essential for the structure, stability and folding of proteins. The identification of intramolecular hydrogen bonds, however, is challenging, in particular in transiently folded states. Here we studied the presence of intramolecular hydrogen bonds in the folding nucleus of the coiled-coil structure of the GCN4 leucine zipper....
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04-18-2014 01:35 PM
Characterization of Mapcho Bicelles - Model Membranes for the NMR Study of Membrane Proteins and Peptides
Characterization of Mapcho Bicelles - Model Membranes for the NMR Study of Membrane Proteins and Peptides
Publication date: 28 January 2014
Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br>
Author(s): Maïwenn Beaugrand , Alexandre A. Arnold , Philip T.F. Williamson , Isabelle Marcotte</br>
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01-29-2014 12:50 AM
Improved accuracy in measuring one-bond and two-bond 15N,13Cα coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy
Improved accuracy in measuring one-bond and two-bond 15N,13Cα coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy
Abstract An extension to HN(CO-α/β-N,Cα-J)-TROSY (Permi and Annila in J Biomol NMR 16:221â??227, 2000) is proposed that permits the simultaneous determination of the four coupling constants 1 J Nâ?²(i)Cα(i), 2 J HN(i)Cα(i), 2 J Cα(iâ??1)Nâ?²(i), and 3 J Cα(iâ??1)HN(i) in 15N,13C-labeled proteins. Contrasting the original scheme, in which two separate subspectra exhibit the 2 J CαNâ?² coupling as inphase and antiphase splitting (IPAP), we...
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06-10-2011 01:41 AM
Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR.
Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR.
Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR.
J Magn Reson. 2011 Mar 21;
Authors: Schanda P, Meier BH, Ernst M
The accurate experimental determination of dipolar-coupling constants for one-bond heteronuclear dipolar couplings in solids is a key for the quantification of the amplitudes of motional processes. Averaging of the dipolar coupling reports on motions on time scales up to the inverse of the coupling...
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04-13-2011 11:57 PM
Accurate Measurement of One-Bond H-X Heteronuclear Dipolar Couplings in MAS Solid-State NMR
Accurate Measurement of One-Bond H-X Heteronuclear Dipolar Couplings in MAS Solid-State NMR
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 21 March 2011</br>
Paul, Schanda , Beat H., Meier , Matthias, Ernst</br>
The accurate experimental determination of dipolar-coupling constants for one-bond heteronuclear dipolar couplings in solids is a key for the quantification of the amplitudes of motional processes. Averaging of the dipolar coupling reports on motions on time scales up to the inverse of the coupling constant, in...
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03-22-2011 07:30 AM
[NMR paper] Rapid amide proton exchange rates in peptides and proteins measured by solvent quench
Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.
Protein Sci. 1995 Apr;4(4):804-14
Authors: Zhang YZ,...
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08-22-2010 03:41 AM
[Question from NMRWiki Q&A forum] Please suggest model proteins and peptides for NMR
Please suggest model proteins and peptides for NMR
do you know any model proteins except lysozyme suitable for nmr experiments?
Check if somebody has answered this question on NMRWiki QA forum
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08-22-2010 02:30 AM
HNCO-based measurement of one-bond amide 15N-1H couplings with optimized precision
Abstract A pair of 3D HNCO-based experiments have been developed with the aim of optimizing the precision of measurement of 1JNH couplings. Both pulse sequences record 1JNH coupling evolution during the entire constant time interval that 15N magnetization is dephasing or rephasing with respect to the directly bonded 13Câ?² nucleus, with 15N13Câ?² multiple quantum coherence maintained during the 13Câ?² evolution period. The first experiment, designed for smaller proteins, produces an apparent doubling of the 1JNH coupling without any accompanying increases in line width. The second experiment...