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Hydrogen-deuterium exchange proteins

Burns-Hamuro L., Hamuro Y, Kim J., Sigala P., Fayos R., Stranz D., Jennings P., Taylor S., Woods V.L. Jr Distinct interaction modes of an AKAP bound to two regulatory subunit isoforms of protein kinase A revealed by amide hydrogen/ deuterium exchange. Protein Sci. [Pg.396]

Hofstadler, S.A. Sannes-Lowery, K.A. Griffey, R.H. Enhanced Gas-Phase Hydrogen-Deuterium Exchange of Oligonucleotide and Protein Ions Stored in an External Multipole Ion Reservoir. J. Mass Spectrom. 2000, 55, 62-70. [Pg.187]

Quantification of Protein-Ligand Interactions in Solution by Hydrogen/Deuterium Exchange (PLIMSTEX)... [Pg.341]

Hamuro, Y. Coales, S.J. Southern, M.R. Nemeth-Cawley, J.F. Stranz, D.D. Rod, G.P. Rapid analysis of protein structure and dynamics by hydrogen/deuterium exchange mass spectrometry. J. Biomol. Tech. 2003,... [Pg.375]

Chalmers, M.J. Busby, S.A. Pascal, B.D. He, Y. Hendrickson, C.L. Marshall, A.G. Griffin, P.R. Probing protein ligand interactions by automated hydrogen/deuterium exchange mass spectrometry. Anal. Chem. 2006. [Pg.375]

Protein-targeting Drug Discovery Guided by Hydrogen/Deuterium Exchange Mass Spectrometry (DXMS)... [Pg.377]

Woods V.L. Jr Dissecting interdomain communication within cAPK regulatory subunit type llbeta using enhanced amide hydrogen/ deuterium exchange mass spectrometry (DXMS). Protein Sci. [Pg.395]

Andersen M.D., Shaffer J., Jennings P.A., Adams J.A. Structural characterization of protein kinase A as a function of nucleotide binding. Hydrogen-deuterium exchange studies using matrix-assisted laser desorption ionization-time of flight mass spectrometry detection. J. Biol. Chem. 2001, 276, 14204-14211. [Pg.395]

Jr Mapping intersubrmit interactions of the regulatory subunit (Rla) in the type 1 holoenzyme of protein kinase A by amide hydrogen/deuterium exchange mass spectrometry (DXMS). J. Mol. Biol. 2004, 340, 1185-1196. [Pg.396]

Pantazatos D., Kim J.S., Klock H.E., Stevens R.C., Wilson LA., Lesley S.A., Woods V.L. Jr Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS. Proc. Natl Acad. Sci. USA 2004, 101, 751-756. [Pg.397]

Englander J., Del Mar C., Li W, Englander S., Kim J., Stranz D., Hamuro Y., Woods Jr. V. Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry. Proc. Natl Acad. Sci. USA 2003, 100, 7057-7062. [Pg.397]

Hamuro Y, Coales S.J., Morrow J., Griffin P.R., Southern M.R., Weber P.C. Application of hydrogen/ deuterium-exchange to p38 mitogen-activated protein kinase. Am. Biotechnol. Lab. (in press). [Pg.398]

Pan J, Rintala-Dempsey AC, Li Y, Shaw GS, Konermann L. 2006. Folding kinetics of the S100A11 protein dimer studied by time-resolved electrospray mass spectrometry and pulsed hydrogen-deuterium exchange. Biochemistry 45(9) 3005-3013. [Pg.132]

Fig. 7. Top mass spectra of FHV y-peptide after acetylation. The degree and site of acetylations, determined by tandem mass spectrometry, can be used to characterize surface accessible regions of the peptide. Bottom a viral capsid protein ion generated by ESI undergoes hydrogen-deuterium exchange. The multiple populations of ions generated can help distinguish between multiple conformers present for a capsid protein... Fig. 7. Top mass spectra of FHV y-peptide after acetylation. The degree and site of acetylations, determined by tandem mass spectrometry, can be used to characterize surface accessible regions of the peptide. Bottom a viral capsid protein ion generated by ESI undergoes hydrogen-deuterium exchange. The multiple populations of ions generated can help distinguish between multiple conformers present for a capsid protein...
Contents J.A.Fee Copper Proteins - Systems Containing the Blue Copper Center. -M.F. Dunn Mechanisms of Zinc Ion Catalysis in Small Molecules and Enzymes. - W. Schneider Kinetics and Mechanism of Metalloporphyrin Formation. - M. Orchin, D. M. Bollinger Hydrogen-Deuterium Exchange in Aromatic Compounds. [Pg.161]

The combination of infrared spectroscopy and hydrogen-deuterium exchange is a powerful technique for revealing small differences in protein secondary structure. Few proteins are composed solely of one type of structure, therefore several amide I and amide II frequencies may contribute to any amide I and II band. It is often difficult to resolve all of these frequencies in the difference spectrum, since some of the peaks have bandwidths which are smaller than the amide I or amide II bandwidth and are thus effectively hidden within the main peak. To resolve overlapping bands, second derivative spectra may be generated using a computer programme. The resultant spectrum is presented as absorbance/(wavenumber)2 versus wavenumber. [Pg.209]

Two other methods, hydrogen-deuterium exchange and far ultraviolet spectroscopy, have produced further evidence that some globular proteins in solution are partially helical. Since quantitative estimates of helical content may be made from these measurements, a discussion of their re-... [Pg.484]

Hydrogen-Deuterium Exchange as an Index oj Partial Helical Content in Native Globular Proteins ... [Pg.511]

Higher-Order Structure and Dynamics of FK506-Binding Protein Probed by Backbone Amide Hydrogen/Deuterium Exchange and Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry... [Pg.703]


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Deuterium exchange

Deuterium hydrogen

Deuterium, exchanged

Exchange proteins

Hydrogen deuterium exchange

Hydrogen-deuterium exchang

Hydrogenation deuterium

Protein dynamics hydrogen-deuterium exchange mass

Protein hydrogenation

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