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Volumn 1084, Issue , 2014, Pages 81-99

Probing backbone dynamics with hydrogen/deuterium exchange mass spectrometry

Author keywords

Backbone amide; HDX MS; Hydrogen deuterium exchange; Mass spectrometry; Protein dynamics; Tandem MS MS sequencing

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; COLLISIONALLY ACTIVATED DISSOCIATION; CONFORMATIONAL TRANSITION; DEUTERIUM HYDROGEN EXCHANGE; ELECTROSPRAY MASS SPECTROMETRY; HYDROGEN BOND; MOLECULAR DYNAMICS; MOLECULAR PROBE; PH; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE;

EID: 84934441314     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-658-0_5     Document Type: Article
Times cited : (4)

References (32)
  • 1
    • 33748619206 scopus 로고    scopus 로고
    • An NMR perspective on enzyme dynamics
    • Boehr DD, Dyson HJ, Wright PE (2006) An NMR perspective on enzyme dynamics. Chem Rev 106(8):3055-3079
    • (2006) Chem Rev , vol.106 , Issue.8 , pp. 3055-3079
    • Boehr, D.D.1    Dyson, H.J.2    Wright, P.E.3
  • 2
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • Volkman BF, Lipson D, Wemmer DE et al (2001) Two-state allosteric behavior in a single-domain signaling protein. Science 291(5512):2429-2433
    • (2001) Science , vol.291 , Issue.5512 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3
  • 3
    • 79551689721 scopus 로고    scopus 로고
    • Protein dynamics and allostery: An NMR view
    • Tzeng SR, Kalodimos CG (2011) Protein dynamics and allostery: an NMR view. Curr Opin Struct Biol 21(1):62-67
    • (2011) Curr Opin Struct Biol , vol.21 , Issue.1 , pp. 62-67
    • Tzeng, S.R.1    Kalodimos, C.G.2
  • 4
    • 0035967856 scopus 로고    scopus 로고
    • Solution-state NMR investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics
    • Rozovsky S, Jogl G, Tong L et al (2001) Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics. J Mol Biol 310(1):271-280
    • (2001) J Mol Biol , vol.310 , Issue.1 , pp. 271-280
    • Rozovsky, S.1    Jogl, G.2    Tong, L.3
  • 5
    • 0141993702 scopus 로고    scopus 로고
    • Protein conformational dynamics probed by single-molecule electron transfer
    • Yang H, Luo G, Karnchanaphanurach P et al (2003) Protein conformational dynamics probed by single-molecule electron transfer. Science 302(5643):262-266
    • (2003) Science , vol.302 , Issue.5643 , pp. 262-266
    • Yang, H.1    Luo, G.2    Karnchanaphanurach, P.3
  • 6
    • 0033813064 scopus 로고    scopus 로고
    • Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy
    • Weiss S (2000) Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy. Nat Struct Biol 7(9):724-729
    • (2000) Nat Struct Biol , vol.7 , Issue.9 , pp. 724-729
    • Weiss, S.1
  • 7
    • 42449110311 scopus 로고    scopus 로고
    • Amide i two-dimensional infrared spectroscopy of proteins
    • Ganim Z, Chung HS, Smith AW et al (2008) Amide I two-dimensional infrared spectroscopy of proteins. Acc Chem Res 41(3):432-441
    • (2008) Acc Chem Res , vol.41 , Issue.3 , pp. 432-441
    • Ganim, Z.1    Chung, H.S.2    Smith, A.W.3
  • 8
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo JL, Goni FM (1999) Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog Biophys Mol Biol 72(4):367-405
    • (1999) Prog Biophys Mol Biol , vol.72 , Issue.4 , pp. 367-405
    • Arrondo, J.L.1    Goni, F.M.2
  • 9
    • 9744270012 scopus 로고    scopus 로고
    • Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry
    • Busenlehner LS, Armstrong RN(2005) Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry. Arch Biochem Biophys 433(1):34-46
    • (2005) Arch Biochem Biophys , vol.433 , Issue.1 , pp. 34-46
    • Busenlehner, L.S.1    Armstrong, R.N.2
  • 10
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Zhang Z, Smith DL (1993) Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation. Protein Sci 2(4):522-531
    • (1993) Protein Sci , vol.2 , Issue.4 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 11
    • 0037059032 scopus 로고    scopus 로고
    • Submolecular cooperativity produces multistate protein unfolding and refolding
    • Englander SW, Mayne L, Rumbley JN (2002) Submolecular cooperativity produces multistate protein unfolding and refolding. Biophys Chem 101-102:57-65
    • (2002) Biophys Chem , vol.101-102 , pp. 57-65
    • Englander, S.W.1    Mayne, L.2    Rumbley, J.N.3
  • 12
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • Konermann L, Pan J, Liu YH (2011) Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem Soc Rev 40(3):1224-1234
    • (2011) Chem Soc Rev , vol.40 , Issue.3 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.H.3
  • 13
    • 0037214137 scopus 로고    scopus 로고
    • Protein hydrogen exchange mechanism: Local fluctuations
    • Maity H, Lim WK, Rumbley JN et al (2003) Protein hydrogen exchange mechanism: local fluctuations. Protein Sci 12(1):153-160
    • (2003) Protein Sci , vol.12 , Issue.1 , pp. 153-160
    • Maity, H.1    Lim, W.K.2    Rumbley, J.N.3
  • 14
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander SW, Kallenbach NR (1983) Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q Rev Biophys 16(4):521-655
    • (1983) Q Rev Biophys , vol.16 , Issue.4 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 15
    • 0015514380 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Molday RS, Englander SW, Kallen RG (1972) Primary structure effects on peptide group hydrogen exchange. Biochemistry 11(2):150-158
    • (1972) Biochemistry , vol.11 , Issue.2 , pp. 150-158
    • Molday, R.S.1    Englander, S.W.2    Kallen, R.G.3
  • 16
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai Y, Milne JS, Mayne L et al (1993) Primary structure effects on peptide group hydrogen exchange. Proteins 17(1):75-86
    • (1993) Proteins , vol.17 , Issue.1 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3
  • 17
    • 0031018084 scopus 로고    scopus 로고
    • Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry
    • Smith DL, Deng Y, Zhang Z (1997) Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry. J Mass Spectrom 32(2):135-146
    • (1997) J Mass Spectrom , vol.32 , Issue.2 , pp. 135-146
    • Smith, D.L.1    Deng, Y.2    Zhang, Z.3
  • 18
    • 43149125442 scopus 로고    scopus 로고
    • Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry
    • Suchanova B, Tuma R (2008) Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry. Microb Cell Fact 7:12
    • (2008) Microb Cell Fact , vol.7 , pp. 12
    • Suchanova, B.1    Tuma, R.2
  • 19
    • 75749148378 scopus 로고    scopus 로고
    • Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry
    • Chapter 17, Unit 17
    • Morgan CR, Engen JR (2009) Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry. Curr Protoc Protein Sci 16:11-17, Chapter 17, Unit 17
    • (2009) Curr Protoc Protein Sci , vol.16 , pp. 11-17
    • Morgan, C.R.1    Engen, J.R.2
  • 20
    • 80052033624 scopus 로고    scopus 로고
    • Protein identification using MS/MS data
    • Cottrell JS (2011) Protein identification using MS/MS data. J Proteomics 74(10):1842-1851
    • (2011) J Proteomics , vol.74 , Issue.10 , pp. 1842-1851
    • Cottrell, J.S.1
  • 21
    • 79954629044 scopus 로고    scopus 로고
    • MSTools: Web based application for visualization and presentation of HXMS data
    • Kavan D, Man P (2011) MSTools: Web based application for visualization and presentation of HXMS data. Int J Mass Spectrom 302:53-58
    • (2011) Int J Mass Spectrom , vol.302 , pp. 53-58
    • Kavan, D.1    Man, P.2
  • 22
    • 79951518978 scopus 로고    scopus 로고
    • HDXanalyzer: A novel package for statistical analysis of protein structure dynamics
    • Liu S, Liu L, Uzuner U et al (2011) HDXanalyzer: a novel package for statistical analysis of protein structure dynamics. BMC Bioinformatics 12(Suppl 1):S43
    • (2011) BMC Bioinformatics , vol.12 , Issue.SUPPL.1
    • Liu, S.1    Liu, L.2    Uzuner, U.3
  • 23
    • 33751337111 scopus 로고    scopus 로고
    • Semiautomated data processing of hydrogen exchange mass spectra using HX-Express
    • Weis DD, Engen JR, Kass IJ (2006) Semiautomated data processing of hydrogen exchange mass spectra using HX-Express. J Am Soc Mass Spectrom 17(12):1700-1703
    • (2006) J Am Soc Mass Spectrom , vol.17 , Issue.12 , pp. 1700-1703
    • Weis, D.D.1    Engen, J.R.2    Kass, I.J.3
  • 24
    • 34249341670 scopus 로고    scopus 로고
    • The Deuterator: Software for the determination of backbone amide deuterium levels from H/D exchange MS data
    • Pascal BD, Chalmers MJ, Busby SA et al (2007) The Deuterator: software for the determination of backbone amide deuterium levels from H/D exchange MS data. BMC Bioinformatics 8:156
    • (2007) BMC Bioinformatics , vol.8 , pp. 156
    • Pascal, B.D.1    Chalmers, M.J.2    Busby, S.A.3
  • 25
    • 0242386421 scopus 로고    scopus 로고
    • Use of different proteases working in acidic conditions to improve sequence coverage and resolution in hydrogen/deuterium exchange of large proteins
    • Cravello L, Lascoux D, Forest E (2003) Use of different proteases working in acidic conditions to improve sequence coverage and resolution in hydrogen/deuterium exchange of large proteins. Rapid Commun Mass Spectrom 17 (21):2387-2393
    • (2003) Rapid Commun Mass Spectrom , vol.17 , Issue.21 , pp. 2387-2393
    • Cravello, L.1    Lascoux, D.2    Forest, E.3
  • 26
    • 0028609328 scopus 로고
    • Surfactant effects on protein structure examined by electrospray ionization mass spectrometry
    • Loo RR, Dales N, Andrews PC (1994) Surfactant effects on protein structure examined by electrospray ionization mass spectrometry. Protein Sci 3(11):1975-1983
    • (1994) Protein Sci , vol.3 , Issue.11 , pp. 1975-1983
    • Loo, R.R.1    Dales, N.2    Andrews, P.C.3
  • 27
    • 0036463721 scopus 로고    scopus 로고
    • Hydrogen exchange-mass spectrometry: Optimization of digestion conditions
    • Wang L, Pan H, Smith DL (2002) Hydrogen exchange-mass spectrometry: optimization of digestion conditions. Mol Cell Proteomics 1 (2):132-138
    • (2002) Mol Cell Proteomics , vol.1 , Issue.2 , pp. 132-138
    • Wang, L.1    Pan, H.2    Smith, D.L.3
  • 28
    • 30644469415 scopus 로고    scopus 로고
    • Molecular weight determination of peptides and proteins by ESI and MALDI
    • Strupat K (2005) Molecular weight determination of peptides and proteins by ESI and MALDI. Methods Enzymol 405:1-36
    • (2005) Methods Enzymol , vol.405 , pp. 1-36
    • Strupat, K.1
  • 29
    • 79954631125 scopus 로고    scopus 로고
    • Analysis of human ferrochelatase iron binding via amide hydrogen/deuterium exchange mass spectrometry
    • Asuru AP, Busenlehner LS (2011) Analysis of human ferrochelatase iron binding via amide hydrogen/deuterium exchange mass spectrometry. Intl J Mass Spectrom 302:76-84
    • (2011) Intl J Mass Spectrom , vol.302 , pp. 76-84
    • Asuru, A.P.1    Busenlehner, L.S.2
  • 30
    • 84866103277 scopus 로고    scopus 로고
    • Dissection of porphyrin-induced conformational dynamics in the heme biosynthesis enzyme ferrochelatase
    • Asuru AP, An M, Busenlehner LS (2012) Dissection of porphyrin-induced conformational dynamics in the heme biosynthesis enzyme ferrochelatase. Biochemistry 51(36): 7116-7127
    • (2012) Biochemistry , vol.51 , Issue.36 , pp. 7116-7127
    • Asuru, A.P.1    An, M.2    Busenlehner, L.S.3
  • 31
    • 33750282788 scopus 로고    scopus 로고
    • Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase
    • Busenlehner LS, Salomonsson L, Brzezinski P et al (2006) Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase. Proc Natl Acad Sci USA 103(42):15398-15403
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.42 , pp. 15398-15403
    • Busenlehner, L.S.1    Salomonsson, L.2    Brzezinski, P.3
  • 32
    • 4444316044 scopus 로고    scopus 로고
    • Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase1
    • Busenlehner LS, Codreanu SG, Holm PJ et al (2004) Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase1. Biochemistry 43(35):11145-11152
    • (2004) Biochemistry , vol.43 , Issue.35 , pp. 11145-11152
    • Busenlehner, L.S.1    Codreanu, S.G.2    Holm, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.