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Volumn 20, Issue 8, 2009, Pages 1514-1517

Protein Conformations Can Be Probed in Top-Down HDX MS Experiments Utilizing Electron Transfer Dissociation of Protein Ions Without Hydrogen Scrambling

Author keywords

[No Author keywords available]

Indexed keywords

DENATURING CONDITIONS; DEUTERIUM CONTENT; ELECTRON-TRANSFER DISSOCIATION; FLEXIBLE SEGMENTS; FLUORANTHENE; FRAGMENT IONS; GASPHASE; HIGHER-ORDER STRUCTURE; HYDROGEN SCRAMBLING; HYDROGEN/DEUTERIUM EXCHANGE; INTACT PROTEINS; ISOTOPIC LABELING; LOCAL INFORMATION; N-TERMINAL; PROTEIN CONFORMATION; PROTEIN IONS; PROTEIN MOLECULES; PROTEIN SEGMENTS; RADICAL ANIONS; TOPDOWN;

EID: 67650763014     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2009.04.006     Document Type: Article
Times cited : (121)

References (17)
  • 1
    • 0036463721 scopus 로고    scopus 로고
    • Hydrogen exchange-mass spectrometry: Optimization of digestion conditions
    • Wang L., Pan H., and Smith D.L. Hydrogen exchange-mass spectrometry: Optimization of digestion conditions. Mol. Cell. Proteomics. 1 (2002) 132-138
    • (2002) Mol. Cell. Proteomics. , vol.1 , pp. 132-138
    • Wang, L.1    Pan, H.2    Smith, D.L.3
  • 2
    • 0036290571 scopus 로고    scopus 로고
    • Crossing the phase boundary to study protein dynamics and function: Combination of amide hydrogen exchange in solution and ion fragmentation in the gas phase
    • Kaltashov I.A., and Eyles S.J. Crossing the phase boundary to study protein dynamics and function: Combination of amide hydrogen exchange in solution and ion fragmentation in the gas phase. J. Mass Spectrom. 37 (2002) 557-565
    • (2002) J. Mass Spectrom. , vol.37 , pp. 557-565
    • Kaltashov, I.A.1    Eyles, S.J.2
  • 3
    • 2942650157 scopus 로고    scopus 로고
    • Is there hydrogen scrambling in the gas phase?. Energetic and structural determinants of proton mobility within protein ions
    • Hoerner J.K., Xiao H., Dobo A., and Kaltashov I.A. Is there hydrogen scrambling in the gas phase?. Energetic and structural determinants of proton mobility within protein ions. J. Am. Chem. Soc. 126 (2004) 7709-7717
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 7709-7717
    • Hoerner, J.K.1    Xiao, H.2    Dobo, A.3    Kaltashov, I.A.4
  • 4
    • 19444384291 scopus 로고    scopus 로고
    • Transient structural disorder as a facilitator of protein-ligand binding: Native H/D exchange-mass spectrometry study of cellular retinoic acid binding protein I
    • Xiao H., and Kaltashov I.A. Transient structural disorder as a facilitator of protein-ligand binding: Native H/D exchange-mass spectrometry study of cellular retinoic acid binding protein I. J. Am. Soc. Mass Spectrom. 16 (2005) 869-879
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 869-879
    • Xiao, H.1    Kaltashov, I.A.2
  • 5
    • 23944509008 scopus 로고    scopus 로고
    • Structural and dynamic characteristics of a partially folded state of ubiquitin revealed by hydrogen exchange mass spectrometry
    • Hoerner J.K., Xiao H., and Kaltashov I.A. Structural and dynamic characteristics of a partially folded state of ubiquitin revealed by hydrogen exchange mass spectrometry. Biochemistry 44 (2005) 11286-11294
    • (2005) Biochemistry , vol.44 , pp. 11286-11294
    • Hoerner, J.K.1    Xiao, H.2    Kaltashov, I.A.3
  • 6
    • 0037130674 scopus 로고    scopus 로고
    • Factors affecting gas-phase deuterium scrambling in peptide ions and their implications for protein structure determination
    • Demmers J.A., Rijkers D.T., Haverkamp J., Killian J.A., and Heck A.J. Factors affecting gas-phase deuterium scrambling in peptide ions and their implications for protein structure determination. J. Am. Chem. Soc. 124 (2002) 11191-11198
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11191-11198
    • Demmers, J.A.1    Rijkers, D.T.2    Haverkamp, J.3    Killian, J.A.4    Heck, A.J.5
  • 7
    • 33846233476 scopus 로고    scopus 로고
    • Hydrogen/deuterium scrambling during quadrupole time-of-flight MS/MS analysis of a zinc-binding protein domain
    • Ferguson P.L., Pan J., Wilson D.J., Dempsey B., Lajoie G., Shilton B., and Konermann L. Hydrogen/deuterium scrambling during quadrupole time-of-flight MS/MS analysis of a zinc-binding protein domain. Anal. Chem. 79 (2007) 153-160
    • (2007) Anal. Chem. , vol.79 , pp. 153-160
    • Ferguson, P.L.1    Pan, J.2    Wilson, D.J.3    Dempsey, B.4    Lajoie, G.5    Shilton, B.6    Konermann, L.7
  • 8
    • 38649092998 scopus 로고    scopus 로고
    • Electron capture dissociation proceeds with a low degree of intramolecular migration of peptide amide hydrogens
    • Rand K.D., Adams C.M., Zubarev R.A., and Jørgensen T.J.D. Electron capture dissociation proceeds with a low degree of intramolecular migration of peptide amide hydrogens. J. Am. Chem. Soc. 130 (2008) 1341-1349
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 1341-1349
    • Rand, K.D.1    Adams, C.M.2    Zubarev, R.A.3    Jørgensen, T.J.D.4
  • 9
    • 51349168541 scopus 로고    scopus 로고
    • Electron capture dissociation of electrosprayed protein ions for spatially resolved hydrogen exchange measurements
    • Pan J., Han J., Borchers C.H., and Konermann L. Electron capture dissociation of electrosprayed protein ions for spatially resolved hydrogen exchange measurements. J. Am. Chem. Soc. 130 (2008) 11574-11575
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11574-11575
    • Pan, J.1    Han, J.2    Borchers, C.H.3    Konermann, L.4
  • 11
    • 67749127567 scopus 로고    scopus 로고
    • Electron transfer dissociation facilitates the measurement of deuterium incorporation into selectively labeled peptides with single residue resolution
    • Zehl M., Rand K.D., Jensen O.N., and Jorgensen T.J. Electron transfer dissociation facilitates the measurement of deuterium incorporation into selectively labeled peptides with single residue resolution. J. Am. Chem. Soc. 130 (2008) 17453-17459
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 17453-17459
    • Zehl, M.1    Rand, K.D.2    Jensen, O.N.3    Jorgensen, T.J.4
  • 14
    • 0034716309 scopus 로고    scopus 로고
    • Protein conformational stability probed by Fourier transform ion cyclotron resonance mass spectrometry
    • Eyles S.J., Speir P., Kruppa G., Gierasch L.M., and Kaltashov I.A. Protein conformational stability probed by Fourier transform ion cyclotron resonance mass spectrometry. J. Am. Chem. Soc. 122 (2000) 495-500
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 495-500
    • Eyles, S.J.1    Speir, P.2    Kruppa, G.3    Gierasch, L.M.4    Kaltashov, I.A.5
  • 16
    • 35048872147 scopus 로고    scopus 로고
    • Effects of cation charge-site identity and position on electron-transfer dissociation of polypeptide cations
    • Xia Y., Gunawardena H.P., Erickson D.E., and McLuckey S.A. Effects of cation charge-site identity and position on electron-transfer dissociation of polypeptide cations. J. Am. Chem. Soc. 129 (2007) 12232-12243
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12232-12243
    • Xia, Y.1    Gunawardena, H.P.2    Erickson, D.E.3    McLuckey, S.A.4
  • 17
    • 33750367908 scopus 로고    scopus 로고
    • Extraction of local hydrogen exchange data from HDX CAD MS measurements by deconvolution of isotopic distributions of fragment ions
    • 1543-1451
    • Abzalimov R.R., and Kaltashov I.A. Extraction of local hydrogen exchange data from HDX CAD MS measurements by deconvolution of isotopic distributions of fragment ions. J. Am. Soc. Mass Spectrom. 17 (2006) 1543-1451
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17
    • Abzalimov, R.R.1    Kaltashov, I.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.