Related ArticlesAn antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR.
Science. 1990 Aug 17;249(4970):755-9
Authors: Paterson Y, Englander SW, Roder H
The interaction of a protein antigen, horse cytochrome c (cyt c), with a monoclonal antibody has been studied by hydrogen-deuterium (H-D) exchange labeling and two-dimensional nuclear magnetic resonance (2D NMR) methods. The H-exchange rate of residues in three discontiguous regions of the cyt c polypeptide backbone was slowed by factors up to 340-fold in the antibody-antigen complex compared with free cyt c. The protected residues, 36 to 38, 59, 60, 64 to 67, 100, and 101, and their hydrogen-bond acceptors, are brought together in the three-dimensional structure to form a contiguous, largely exposed protein surface with an area of about 750 square angstroms. The interaction site determined in this way is consistent with prior epitope mapping studies and includes several residues that were not previously identified. The hydrogen exchange labeling approach can be used to map binding sites on small proteins in antibody-antigen complexes and may be applicable to protein-protein and protein-ligand interactions in general.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Biophys J. 2011 Aug 3;101(3):L23-L25
Authors: Wang S, Shi L, Kawamura I, Brown LS, Ladizhansky V
Solid-state NMR spectroscopy is an efficient tool for following conformational dynamics of membrane proteins at atomic resolution. We used this technique for the site-specific...
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[NMR paper] Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c
Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c under strongly destabilizing conditions.
Related Articles Stopped-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...
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NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by t
NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Z? domains of yatapoxvirus E3L.
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FEBS Lett. 2010 Oct 8;
Authors: Lee EH, Seo YJ, Ahn HC, Kang YM, Kim HE, Lee YM, Choi BS, Lee JH
The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus,...
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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] The substrate binding site of human liver cytochrome P450 2C9: an NMR study.
The substrate binding site of human liver cytochrome P450 2C9: an NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The substrate binding site of human liver cytochrome P450 2C9: an NMR study.
Biochemistry. 1997 Oct 21;36(42):12672-82
Authors: Poli-Scaife S, Attias R, Dansette PM, Mansuy D
Purified recombinant human liver cytochrome P450 2C9 was produced, from expression of the corresponding cDNA in yeast, in quantities large enough for UV-visible and 1H NMR experiments. Its...
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[NMR paper] Mechanism of hydrogen-deuterium exchange in trp repressor studied by 1H-15N NMR.
Mechanism of hydrogen-deuterium exchange in trp repressor studied by 1H-15N NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Mechanism of hydrogen-deuterium exchange in trp repressor studied by 1H-15N NMR.
J Mol Biol. 1995 Nov 3;253(4):576-89
Authors: Finucane MD, Jardetzky O
Amide proton exchange rates have been measured for fast-exchanging amides in trp aporepressor, and compared with the rates measured in the holorepressor. The results indicate that the presence...
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[NMR paper] Effect of antibody binding on protein motions studied by hydrogen-exchange labeling a
Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR.
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Biochemistry. 1992 Nov 10;31(44):10678-85
Authors: Mayne L, Paterson Y, Cerasoli D, Englander SW
We have used hydrogen-exchange labeling detected by 2D NMR to study antibody-protein interactions for two monoclonal antibodies raised against horse cytochrome c. The data show that these antibodies bind mainly to the...
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[NMR paper] Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR
Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR.
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Biochemistry. 1990 Nov 20;29(46):10433-7
Authors: Jeng MF, Englander SW, Elöve GA, Wand AJ, Roder H
Hydrogen exchange and two-dimensional nuclear magnetic resonance (2D NMR) techniques were used to characterize the structure of oxidized horse cytochrome c at acid pH and high ionic strength. Under these conditions, cytochrome c is known to assume a...
An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensi
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