Related ArticlesDefining protein ensembles with native-state NH exchange: kinetics of interconversion and cooperative units from combined NMR and MS analysis.
J Mol Biol. 1999 Jan 22;285(3):1265-75
Authors: Arrington CB, Teesch LM, Robertson AD
Previous studies of native-state peptide hydrogen atom (NH) exchange in turkey ovomucoid third domain (OMTKY3) yielded the thermodynamics and kinetics of unfolding and folding for the 14 slowest-exchanging peptide hydrogen atoms (NHs). Unfolding rate constants and free energies for nine of the NHs are very similar, suggesting that these NHs exchange during a single cooperative unfolding event. Electrospray ionization mass spectrometry (ESI-MS) has been used to test this hypothesis. ESI-MS data and MS peak simulations suggest that this hypothesis is incorrect: in spite of the similarity in their unfolding rate constants, only three to five of the nine residues exchange in a cooperative manner. Thus, residues with similar thermodynamics and kinetics of exchange are probably involved in multiple conformational equilibria. Overall, combined NMR and MS analysis of NH exchange provides a rich and complex picture of the ensemble properties of native proteins.
[NMR paper] Measuring pK(a) values in protein folding transition state ensembles by NMR spectrosc
Measuring pK(a) values in protein folding transition state ensembles by NMR spectroscopy.
Related Articles Measuring pK(a) values in protein folding transition state ensembles by NMR spectroscopy.
J Am Chem Soc. 2005 Jun 29;127(25):8904-5
Authors: Tollinger M, Kay LE, Forman-Kay JD
Protein folding kinetic data have been obtained for the marginally stable N-terminal SH3 domain of the Drosophila protein drk as a function of pH in order to investigate the electrostatic properties of Asp8 in the folding transition state ensemble. The slow exchange...
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[NMR paper] NMR studies on Cu(II)-peptide complexes: exchange kinetics and determination of struc
NMR studies on Cu(II)-peptide complexes: exchange kinetics and determination of structures in solution.
Related Articles NMR studies on Cu(II)-peptide complexes: exchange kinetics and determination of structures in solution.
Mol Biosyst. 2005 May;1(1):79-84
Authors: Gaggelli E, Kozlowski H, Valensin D, Valensin G
The interaction of copper(II) with histidine containing peptides has recently acquired renewed interest following the established link between abnormal protein behaviour in neurodegenerative processes and unpaired copper homeostasis....
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[NMR paper] An NMR method for studying the kinetics of metal exchange in biomolecular systems.
An NMR method for studying the kinetics of metal exchange in biomolecular systems.
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J Biomol NMR. 2002 Aug;23(4):303-9
Authors: Barbieri R, Hore PJ, Luchina C, Pierattelli R
The kinetics of lanthanide (III) exchange for calcium(II) in the C-terminal EF-hand of the protein calbindin D9k have been studied by one-dimensional (1D) stopped-flow NMR. By choosing a paramagnetic lanthanide (Ce3+), kinetics in the sub-second range can be easily measured....
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[NMR paper] Hydrogen exchange properties of proteins in native and denatured states monitored by
Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and 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 Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.
Protein Sci. 1997 Jun;6(6):1316-24
Authors: Chung EW,...
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[NMR paper] Hydrogen exchange properties of proteins in native and denatured states monitored by
Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and 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 Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.
Protein Sci. 1997 Jun;6(6):1316-24
Authors: Chung EW,...
[NMR paper] Hydrogen exchange kinetics in a membrane protein determined by 15N NMR spectroscopy:
Hydrogen exchange kinetics in a membrane protein determined by 15N NMR spectroscopy: use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein.
Related Articles Hydrogen exchange kinetics in a membrane protein determined by 15N NMR spectroscopy: use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein.
Biochemistry. 1990 Jul 3;29(26):6303-13
Authors: Henry GD, Sykes BD
The coat protein of the filamentous coliphage M13 is a 50-residue polypeptide which spans the...
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Structure-based protein NMR assignments using native structural ensembles
Structure-based protein NMR assignments using native structural ensembles
Mehmet Serkan Apaydın, Vincent Conitzer and Bruce Randall Donald
Journal of Biomolecular NMR; 2008; 40(4); pp 263-276
Abstract:
An important step in NMR protein structure determination is the assignment of resonances and NOEs to corresponding nuclei. Structure-based assignment (SBA) uses a model structure (“template”) for the target protein to expedite this process. Nuclear vector replacement (NVR) is an SBA framework that combines multiple sources of NMR data (chemical shifts, RDCs, sparse NOEs, amide exchange...
Defining protein ensembles with native-state NH exchange: kinetics of interconversion
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