Related ArticlesCarbonyl 13C-detect solution-state protein NMR experiments to circumvent amide-solvent exchange broadening: Application to ?2-microglobulin.
Biochim Biophys Acta Proteins Proteom. 2020 Dec 23;:140593
Authors: Yoshimura Y, So M, Miyanoiri Y
Abstract
The 15N1H heteronuclear single-quantum correlation (HSQC) technique in protein NMR spectroscopy suffers from line-broadening effects, such as chemical exchange of labile protons with solvent, and exchange broadening for residues undergoing conformational dynamics. The amide resonance of ?2-microglobulin residue S88 is not observed in the HSQC spectrum but can be obtained through 13C-detect experiments that circumvent the problem of amide-solvent exchange broadening. Line broadening of S88 resonance beyond detection in the HSQC spectrum is not attributed to conformational exchange but rather to solvent exchange occurring on the order of ~103 s-1.
PMID: 33359410 [PubMed - as supplied by publisher]
Exchangeable deuterons introduce artifacts in amide 15 N CEST experiments used to study protein conformational exchange
Exchangeable deuterons introduce artifacts in amide 15 N CEST experiments used to study protein conformational exchange
Abstract
Protein molecules sample different conformations in solution and characterizing these conformations is crucial to understanding protein function. 15N CEST experiments are now routinely used to study slow conformational exchange of protein molecules between a ā??visibleā?? major state and ā??invisibleā?? minor states. These experiments have also been adapted to measure the solvent exchange rates of amide protons by exploiting...
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03-24-2019 10:41 PM
Longitudinal relaxation optimized amide 1 H-CEST experiments for studying slow chemical exchange processes in fully protonated proteins
Longitudinal relaxation optimized amide 1 H-CEST experiments for studying slow chemical exchange processes in fully protonated proteins
Abstract
Chemical Exchange Saturation Transfer (CEST) experiments are increasingly used to study slow timescale exchange processes in biomolecules. Although 15N- and 13C-CEST have been the approaches of choice, the development of spin state selective 1H-CEST pulse sequences that separate the effects of chemical and dipolar exchange significantly increases the utility of 1H-based experiments. Pulse schemes have been...
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03-30-2017 06:42 PM
[NMR paper] Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.
Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.
PLoS One. 2013;8(2):e56467
Authors: Alexandrescu AT
Abstract
Amylin is an endocrine hormone that...
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08-29-2013 01:53 PM
Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N15N and carbonyl 13C13C dipolar recoupling data
Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N15N and carbonyl 13C13C dipolar recoupling data
May 2012
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 218</br>
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Recent structural studies of uniformly 15N, 13C-labeled proteins by solid state nuclear magnetic resonance (NMR) rely principally on two sources of structural restraints: (i) restraints on backbone conformation from isotropic 15N and 13C chemical shifts, based on empirical correlations between chemical shifts and...
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02-03-2013 10:13 AM
Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data
Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Kan-Nian Hu, Wei Qiang, Guillermo A. Bermejo, Charles D. Schwieters, Robert Tycko</br>
Recent structural studies of uniformly 15N,13C-labeled proteins by solid state nuclear magnetic resonance (NMR) rely principally on two sources of structural restraints: (i) restraints on backbone conformation from isotropic 15N and 13C chemical...
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03-10-2012 10:54 AM
[NMR paper] Temperature dependence of protein backbone motion from carbonyl 13C and amide 15N NMR
Temperature dependence of protein backbone motion from carbonyl 13C and amide 15N NMR relaxation.
Related Articles Temperature dependence of protein backbone motion from carbonyl 13C and amide 15N NMR relaxation.
J Magn Reson. 2005 May;174(1):43-53
Authors: Chang SL, Tjandra N
The NMR spin-lattice relaxation rate (R1) and the rotating-frame spin-lattice relaxation rate (R1rho) of amide 15N and carbonyl 13C (13C') of the uniformly 13C- and 15N-labeled ubiquitin were measured at different temperatures and field strengths to investigate the...
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11-25-2010 08:21 PM
[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
15NH/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: a
Abstract Amide solvent exchange rates are regarded as a valuable source of information on structure/dynamics of unfolded (disordered) proteins. Proton-based saturation transfer experiments, normally used to measure solvent exchange, are known to meet some serious difficulties. The problems mainly arise from the need to (1) manipulate water magnetization and (2) discriminate between multiple magnetization transfer pathways that occur within the proton pool. Some of these issues are specific to unfolded proteins. For example, the compensation scheme used to cancel the Overhauser effect in the...
Carbonyl 13C-detect solution-state protein NMR experiments to circumvent amide-solvent exchange broadening: Application to ?2-microglobulin.
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