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Volumn 26, Issue 23, 2012, Pages 2739-2744

Hydrogen scrambling in non-covalent complexes of peptides

Author keywords

[No Author keywords available]

Indexed keywords

DISSOCIATION; ELECTROSPRAY IONIZATION; HYDROGEN; HYDROGEN BONDS; MASS SPECTROMETRY; PEPTIDES;

EID: 84868338341     PISSN: 09514198     EISSN: 10970231     Source Type: Journal    
DOI: 10.1002/rcm.6396     Document Type: Article
Times cited : (9)

References (25)
  • 1
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • L. Konermann, J. Pan, Y. H. Liu,. Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem. Soc. Rev. 2011, 40, 1224.
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1224
    • Konermann, L.1    Pan, J.2    Liu, Y.H.3
  • 2
    • 84863207545 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry: Are we out of the quicksand?
    • R. E. Iacob, J. R. Engen,. Hydrogen exchange mass spectrometry: Are we out of the quicksand? J. Am. Soc. Mass Spectrom. 2012, 23, 1003.
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 1003
    • Iacob, R.E.1    Engen, J.R.2
  • 3
    • 79954634321 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange mass spectrometry and optical spectroscopy as complementary tools for studying the structure and dynamics of a membrane protein
    • Y. Pan, L. Brown, L. Konermann,. Hydrogen/deuterium exchange mass spectrometry and optical spectroscopy as complementary tools for studying the structure and dynamics of a membrane protein. Int. J. Mass Spectrom. 2011, 302, 3.
    • (2011) Int. J. Mass Spectrom. , vol.302 , pp. 3
    • Pan, Y.1    Brown, L.2    Konermann, L.3
  • 4
    • 84856297467 scopus 로고    scopus 로고
    • Crystal structure of the human two-pore domain potassium channel K2P1
    • A. N. Miller, S. B. Long,. Crystal structure of the human two-pore domain potassium channel K2P1. Science 2012, 335, 432.
    • (2012) Science , vol.335 , pp. 432
    • Miller, A.N.1    Long, S.B.2
  • 5
    • 82755176172 scopus 로고    scopus 로고
    • The cystic fibrosis transmembrane conductance regulator (CFTR) three-dimensional structure and localization of a channel gate
    • M. F. Rosenberg, L. P. O'Ryan, G. Hughes, Z. Zhao, L. A. Aleksandrov, J. R. Riordan, R. C. Ford,. The cystic fibrosis transmembrane conductance regulator (CFTR) three-dimensional structure and localization of a channel gate. J. Biol. Chem. 2011, 286, 42647.
    • (2011) J. Biol. Chem. , vol.286 , pp. 42647
    • Rosenberg, M.F.1    O'Ryan, L.P.2    Hughes, G.3    Zhao, Z.4    Aleksandrov, L.A.5    Riordan, J.R.6    Ford, R.C.7
  • 6
    • 80054892557 scopus 로고    scopus 로고
    • Structural stability from solution to the gas phase: Native solution structure of ubiquitin survives analysis in a solvent-free ion mobility mass spectrometry environment
    • T. Wyttenbach, M. T. Bowers,. Structural stability from solution to the gas phase: Native solution structure of ubiquitin survives analysis in a solvent-free ion mobility mass spectrometry environment. J. Phys. Chem. B 2011, 115, 12266.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 12266
    • Wyttenbach, T.1    Bowers, M.T.2
  • 7
    • 29244443271 scopus 로고    scopus 로고
    • Collisional activation by MALDI tandem time-of-flight mass spectrometry induces intramolecular migration of amide hydrogens in protonated peptides
    • T. J. D. Jørgensen, N. Bache, P. Roepstorff, H. GÃ¥rdsvoll, M. Ploug,. Collisional activation by MALDI tandem time-of-flight mass spectrometry induces intramolecular migration of amide hydrogens in protonated peptides. Mol. Cell. Proteomics 2005, 4, 1910.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1910
    • Jørgensen, T.J.D.1    Bache, N.2    Roepstorff, P.3    Gãrdsvoll, H.4    Ploug, M.5
  • 8
    • 84860805088 scopus 로고    scopus 로고
    • Fragmentation hydrogen exchange mass spectrometry: A review of methodology and applications
    • A. Brock,. Fragmentation hydrogen exchange mass spectrometry: A review of methodology and applications. Protein Expression Purification 2012, 84, 19.
    • (2012) Protein Expression Purification , vol.84 , pp. 19
    • Brock, A.1
  • 9
    • 80051552668 scopus 로고    scopus 로고
    • Top-down high-resolution electron capture dissociation mass spectrometry for comprehensive characterization of post-translational modifications in Rhesus monkey cardiac troponin i
    • F. Xu, Q. Xu, X. Dong, M. Guy, H. Guner, T. A. Hacker, Y. Ge,. Top-down high-resolution electron capture dissociation mass spectrometry for comprehensive characterization of post-translational modifications in Rhesus monkey cardiac troponin I. Int. J. Mass Spectrom. 2011, 305, 95.
    • (2011) Int. J. Mass Spectrom. , vol.305 , pp. 95
    • Xu, F.1    Xu, Q.2    Dong, X.3    Guy, M.4    Guner, H.5    Hacker, T.A.6    Ge, Y.7
  • 10
    • 84856690645 scopus 로고    scopus 로고
    • Optimization of electron transfer dissociation via informed selection of reagents and operating parameters
    • P. D. Compton, J. V. Strukl, D. L. Bai, J. Shabanowitz, D. F. Hunt,. Optimization of electron transfer dissociation via informed selection of reagents and operating parameters. Anal. Chem. 2012, 84, 1781.
    • (2012) Anal. Chem. , vol.84 , pp. 1781
    • Compton, P.D.1    Strukl, J.V.2    Bai, D.L.3    Shabanowitz, J.4    Hunt, D.F.5
  • 11
    • 79953704774 scopus 로고    scopus 로고
    • Electron detachment dissociation for top-down mass spectrometry of acidic proteins
    • B. Ganisl, T. Valovka, M. Hartl, M. Taucher, K. Bister, K. Breuker,. Electron detachment dissociation for top-down mass spectrometry of acidic proteins. Chem. Eur. J. 2011, 17, 4460.
    • (2011) Chem. Eur. J. , vol.17 , pp. 4460
    • Ganisl, B.1    Valovka, T.2    Hartl, M.3    Taucher, M.4    Bister, K.5    Breuker, K.6
  • 12
    • 78650881098 scopus 로고    scopus 로고
    • Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides
    • K. Kowalewska, P. Stefanowicz, T. Ruman, T. Fra̧czyk, W. Rode, Z. Szewczuk,. Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides. Biosci. Rep. 2010, 30, 433.
    • (2010) Biosci. Rep. , vol.30 , pp. 433
    • Kowalewska, K.1    Stefanowicz, P.2    Ruman, T.3    Fra̧czyk, T.4    Rode, W.5    Szewczuk, Z.6
  • 13
    • 79952152636 scopus 로고    scopus 로고
    • On the accuracy and limits of peptide fragmentation spectrum prediction
    • S. Li, R. J. Arnold, H. Tang, P. Radivojac,. On the accuracy and limits of peptide fragmentation spectrum prediction. Anal. Chem. 2011, 83, 790.
    • (2011) Anal. Chem. , vol.83 , pp. 790
    • Li, S.1    Arnold, R.J.2    Tang, H.3    Radivojac, P.4
  • 14
    • 14744272834 scopus 로고    scopus 로고
    • Intramolecular migration of amide hydrogens in protonated peptides upon collisional activation
    • T. J. D. Jørgensen, H. GÃ¥rdsvoll, M. Ploug, P. Roepstorff,. Intramolecular migration of amide hydrogens in protonated peptides upon collisional activation. J. Am. Chem. Soc. 2005, 127, 2785.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2785
    • Jørgensen, T.J.D.1    Gãrdsvoll, H.2    Ploug, M.3    Roepstorff, P.4
  • 15
  • 16
    • 79960231733 scopus 로고    scopus 로고
    • The charge ratio between O and N on amide bonds: A new approach to the mobile proton model
    • M. Wang, P. Zhang, W. Zong, Q. Xu, R. Liu,. The charge ratio between O and N on amide bonds: A new approach to the mobile proton model. Spectrochim. Acta Part A 2011, 79, 1915.
    • (2011) Spectrochim. Acta Part A , vol.79 , pp. 1915
    • Wang, M.1    Zhang, P.2    Zong, W.3    Xu, Q.4    Liu, R.5
  • 17
    • 0034055215 scopus 로고    scopus 로고
    • Proton mobility in protonated peptides: A joint molecular orbital and RRKM study
    • I. P. Csonka, B. Paizs, G. Lendvay, S. Suhai,. Proton mobility in protonated peptides: a joint molecular orbital and RRKM study. Rapid Commun. Mass Spectrom. 2000, 14, 417.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 417
    • Csonka, I.P.1    Paizs, B.2    Lendvay, G.3    Suhai, S.4
  • 18
    • 75649131903 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry as a method for studying the high pressure denaturation of proteins
    • P. Stefanowicz, I. Petry-Podgorska, K. Kowalewska, L. Jaremko, M. Jaremko, Z. Szewczuk,. Electrospray ionization mass spectrometry as a method for studying the high pressure denaturation of proteins. Biosci. Rep. 2010, 30, 91.
    • (2010) Biosci. Rep. , vol.30 , pp. 91
    • Stefanowicz, P.1    Petry-Podgorska, I.2    Kowalewska, K.3    Jaremko, L.4    Jaremko, M.5    Szewczuk, Z.6
  • 19
    • 34047144959 scopus 로고    scopus 로고
    • Helices and sheets in vacuo
    • M. F. Jarrold,. Helices and sheets in vacuo. Phys. Chem. Chem. Phys. 2007, 9, 1659.
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 1659
    • Jarrold, M.F.1
  • 20
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • J. A. Loo,. Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom. Rev. 1997, 16, 1.
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 1
    • Loo, J.A.1
  • 21
    • 77951665751 scopus 로고    scopus 로고
    • Methods of the site-selective solid phase synthesis of peptide-derived Amadori products
    • P. Stefanowicz, M. Kijewska, K. Kapczyńska, Z. Szewczuk,. Methods of the site-selective solid phase synthesis of peptide-derived Amadori products. Amino Acids 2010, 38, 881.
    • (2010) Amino Acids , vol.38 , pp. 881
    • Stefanowicz, P.1    Kijewska, M.2    Kapczyńska, K.3    Szewczuk, Z.4
  • 22
    • 78650839196 scopus 로고    scopus 로고
    • Non-covalent dimers of the lysine containing protonated peptide ions in gaseous state: Electrospray ionization mass spectrometric study
    • S. Banerjee, S. Mazumdar,. Non-covalent dimers of the lysine containing protonated peptide ions in gaseous state: electrospray ionization mass spectrometric study. J. Mass. Spectrom. 2010, 45, 1212.
    • (2010) J. Mass. Spectrom. , vol.45 , pp. 1212
    • Banerjee, S.1    Mazumdar, S.2
  • 23
    • 70350507226 scopus 로고    scopus 로고
    • Electrospray: From ions in solution to ions in the gas phase, what we know now
    • P. Kebarle, U. H. Verkerk,. Electrospray: From ions in solution to ions in the gas phase, what we know now. Mass Spectrom. Rev. 2009, 28, 898.
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 898
    • Kebarle, P.1    Verkerk, U.H.2
  • 24
    • 38349125328 scopus 로고    scopus 로고
    • Conformational and noncovalent complexation changes in proteins during electrospray ionization
    • P. Nemes, S. Goyal, A. Vertes,. Conformational and noncovalent complexation changes in proteins during electrospray ionization. Anal. Chem. 2008, 80, 387.
    • (2008) Anal. Chem. , vol.80 , pp. 387
    • Nemes, P.1    Goyal, S.2    Vertes, A.3
  • 25
    • 58249084606 scopus 로고    scopus 로고
    • The Use of ECD/ETD to identify the site of electrostatic interaction in noncovalent complexes
    • S. N. Jackson, S. Dutta, A. S. Woods,. The Use of ECD/ETD to identify the site of electrostatic interaction in noncovalent complexes. J. Am. Soc. Mass Spectrom. 2009, 20, 176.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 176
    • Jackson, S.N.1    Dutta, S.2    Woods, A.S.3


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