Related ArticlesStopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c under strongly destabilizing conditions.
Proteins. 1998 Aug 1;32(2):241-7
Authors: Bhuyan AK, Udgaonkar JB
A procedure to measure exchange rates of fast exchanging protein amide hydrogens by time-resolved NMR spectroscopy following in situ initiation of the reaction by diluting a native protein solution into an exchanging deuterated buffer is described. The method has been used to measure exchange rates of a small set of amide hydrogens of reduced cytochrome c, maintained in a strictly anaerobic atmosphere, in the presence of an otherwise inaccessible range of guanidinium deuterochloride concentrations. The results for the measured protons indicate that hydrogen exchange in the unfolding transition region of cytochrome c reach the EX2 limit, but emphasize the difficulty in interpretation of the exchange mechanism in protein hydrogen exchange studies. Comparison of free energies of structure opening for the measured hydrogens with the global unfolding free energy monitored by far-UV CD measurements has indicated the presence of at least one partially unfolded equilibrium species of reduced cytochrome c. The results provide the first report of measurement of free energy of opening of structure to exchange in the 0-2-kcal/mol range.
Measurement of amide hydrogen exchange rates with the use of radiation damping
Measurement of amide hydrogen exchange rates with the use of radiation damping
Abstract A simple method for measuring amide hydrogen exchange rates is presented, which is based on the selective inversion of water magnetization with the use of radiation damping. Simulations show that accurate exchange rates can be measured despite the complications of radiation damping and cross relaxation to the exchange process between amide and water protons. This method cannot eliminate the contributions of the exchange-relayed NOE and direct NOE to the measured exchange rates, but minimize the...
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[NMR paper] Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H N
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.
Related Articles Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.
Protein Sci. 2000 Jan;9(1):186-93
Authors: Cavagnero S, Thériault Y, Narula SS, Dyson HJ, Wright PE
The hydrogen exchange behavior of exchangeable protons in proteins can provide important information for understanding the principles of protein structure and function. The positions and exchange rates of the slowly-exchanging amide...
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Quantification of protein backbone hydrogen-deuterium exchange rates by solid state N
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy
Abstract We present the quantification of backbone amide hydrogen-deuterium exchange rates (HDX) for immobilized proteins. The experiments make use of the deuterium isotope effect on the amide nitrogen chemical shift, as well as on proton dilution by deuteration. We find that backbone amides in the microcrystalline α-spectrin SH3 domain exchange rather slowly with the solvent (with exchange rates negligible within the individual 15Nâ??T 1 timescales). We observed chemical exchange for 6...
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Quantification of protein backbone hydrogen-deuterium exchange rates by solid state N
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.
Related Articles Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.
J Biomol NMR. 2010 Oct 20;
Authors: Del Amo JM, Fink U, Reif B
We present the quantification of backbone amide hydrogen-deuterium exchange rates (HDX) for immobilized proteins. The experiments make use of the deuterium isotope effect on the amide nitrogen chemical shift, as well as on proton dilution by deuteration. We find that...
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[NMR paper] Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mas
Human recombinant FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from 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 Human recombinant FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR.
Protein Sci. 1997 Oct;6(10):2203-17
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[NMR paper] Characterisation of the electron self-exchange rates in hexametaphosphate-cytochrome-
Characterisation of the electron self-exchange rates in hexametaphosphate-cytochrome-c aggregates measured using high-resolution 1H-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Characterisation of the electron self-exchange rates in hexametaphosphate-cytochrome-c aggregates measured using high-resolution 1H-NMR spectroscopy.
Eur J Biochem. 1991 Aug 1;199(3):553-60
Authors: Concar DW, Whitford D, Williams RJ
...
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[NMR paper] Characterisation of the electron self-exchange rates in hexametaphosphate-cytochrome-
Characterisation of the electron self-exchange rates in hexametaphosphate-cytochrome-c aggregates measured using high-resolution 1H-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Characterisation of the electron self-exchange rates in hexametaphosphate-cytochrome-c aggregates measured using high-resolution 1H-NMR spectroscopy.
Eur J Biochem. 1991 Aug 1;199(3):553-60
Authors: Concar DW, Whitford D, Williams RJ
...
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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...
Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c
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