메뉴 건너뛰기




Volumn 323, Issue 4, 2004, Pages 1134-1138

Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry

Author keywords

2 Hydroxy 5 nitrobenzyl bromide; Koshland's reagent; MALDI TOF mass spectrometry; Protein surface mapping; Tryptophan modification

Indexed keywords

2 HYDROXY 5 NITROBENZYL BROMIDE; AMINO ACID; TRYPTOPHAN;

EID: 4644231769     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.08.217     Document Type: Article
Times cited : (20)

References (22)
  • 2
    • 0032502991 scopus 로고    scopus 로고
    • Protein conformational changes determined by matrix-assisted laser desorption mass spectrometry
    • H.H. Yang, X.C. Li, M. Amft, and J. Grotemeyer Protein conformational changes determined by matrix-assisted laser desorption mass spectrometry Anal. Biochem. 258 1998 118 126
    • (1998) Anal. Biochem. , vol.258 , pp. 118-126
    • Yang, H.H.1    Li, X.C.2    Amft, M.3    Grotemeyer, J.4
  • 3
    • 0030811920 scopus 로고    scopus 로고
    • Probing protein structure using biochemical and biophysical methods Proteolysis, matrix-assisted laser desorption/ionization mass spectrometry, high-performance liquid chromatography and size-exclusion chromatography of p21 (Waf1/Cip1/Sdi1)
    • R.W. Kriwacki, J. Wu, L. Tennant, P.E. Wright, and G. Siuzdak Probing protein structure using biochemical and biophysical methods Proteolysis, matrix-assisted laser desorption/ionization mass spectrometry, high-performance liquid chromatography and size-exclusion chromatography of p21 (Waf1/Cip1/Sdi1) J. Chromatogr. A 777 1997 23 30
    • (1997) J. Chromatogr. a , vol.777 , pp. 23-30
    • Kriwacki, R.W.1    Wu, J.2    Tennant, L.3    Wright, P.E.4    Siuzdak, G.5
  • 4
    • 0033551439 scopus 로고    scopus 로고
    • Substrate and inhibitor-induced conformational changes in the structurally related enzymes UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate 3-phosphate synthase (EPSPS)
    • F. Krekel, C. Oecking, N. Amrhein, and P. Macheroux Substrate and inhibitor-induced conformational changes in the structurally related enzymes UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5- enolpyruvylshikimate 3-phosphate synthase (EPSPS) Biochemistry 38 1999 8864 8878
    • (1999) Biochemistry , vol.38 , pp. 8864-8878
    • Krekel, F.1    Oecking, C.2    Amrhein, N.3    MacHeroux, P.4
  • 6
    • 0031018084 scopus 로고    scopus 로고
    • Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry
    • D.L. Smith, Y. Deng, and Z. Zhang Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry J. Mass Spectrom. 32 1997 135 146
    • (1997) J. Mass Spectrom. , vol.32 , pp. 135-146
    • Smith, D.L.1    Deng, Y.2    Zhang, Z.3
  • 8
    • 0033473760 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization hydrogen/deuterium exchange studies to probe peptide conformational changes
    • I.D. Figueroa, and D.H. Russell Matrix-assisted laser desorption ionization hydrogen/deuterium exchange studies to probe peptide conformational changes J. Am. Soc. Mass Spectrom. 10 1999 719 731
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 719-731
    • Figueroa, I.D.1    Russell, D.H.2
  • 9
    • 0030458684 scopus 로고    scopus 로고
    • Selective biochemical modification of functional residues in recombinant human macrophage colony-stimulating factor β (rhM-CSFβ): Identification by mass spectrometry
    • M.O. Glocker, M. Kalkum, R. Yamamoto, and J. Schreurs Selective biochemical modification of functional residues in recombinant human macrophage colony-stimulating factor β (rhM-CSFβ): identification by mass spectrometry Biochemistry 35 1996 14625 14633
    • (1996) Biochemistry , vol.35 , pp. 14625-14633
    • Glocker, M.O.1    Kalkum, M.2    Yamamoto, R.3    Schreurs, J.4
  • 10
    • 0032032551 scopus 로고    scopus 로고
    • Molecular characterization of a conformational epitope of hen egg white lysozyme by differential chemical modification of immune complexes and mass spectrometric peptide mapping
    • W. Fiedler, C. Borchers, M. Macht, S.O. Deininger, and M. Przybylski Molecular characterization of a conformational epitope of hen egg white lysozyme by differential chemical modification of immune complexes and mass spectrometric peptide mapping Bioconjugate Chem. 9 1998 236 241
    • (1998) Bioconjugate Chem. , vol.9 , pp. 236-241
    • Fiedler, W.1    Borchers, C.2    MacHt, M.3    Deininger, S.O.4    Przybylski, M.5
  • 11
    • 0001579960 scopus 로고
    • An environmentally-sensitive reagent with selectivity for the tryptophan residues in protein
    • D.E. Koshland Jr., Y.D. Karkhanis, and H.G. Latham An environmentally-sensitive reagent with selectivity for the tryptophan residues in protein J. Am. Chem. Soc. 86 1964 1448 1450
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 1448-1450
    • Koshland Jr., D.E.1    Karkhanis, Y.D.2    Latham, H.G.3
  • 12
    • 0001388414 scopus 로고
    • A highly reactive colored reagent with selectivity for the tryptophan residue in protein. 2-hydroxy-5-nitrobenzyl bromide
    • H.R. Horton, and D.E. Koshland Jr. A highly reactive colored reagent with selectivity for the tryptophan residue in protein. 2-hydroxy-5-nitrobenzyl bromide J. Am. Chem. Soc. 87 5 1965 1126 1132
    • (1965) J. Am. Chem. Soc. , vol.87 , Issue.5 , pp. 1126-1132
    • Horton, H.R.1    Koshland Jr., D.E.2
  • 13
    • 0014666758 scopus 로고
    • The chemistry of the modification of tryptophan with 2-hydroxy-5- nitrobenzyl bromide
    • G.M. Loudon, D. Portsmouth, A. Lukton, and D.E. Koshland Jr. The chemistry of the modification of tryptophan with 2-hydroxy-5-nitrobenzyl bromide J. Am. Chem. Soc. 91 10 1969 2792 2794
    • (1969) J. Am. Chem. Soc. , vol.91 , Issue.10 , pp. 2792-2794
    • Loudon, G.M.1    Portsmouth, D.2    Lukton, A.3    Koshland Jr., D.E.4
  • 14
    • 0344121217 scopus 로고    scopus 로고
    • Tryptophan modification by 2-hydroxy-5-nitrobenzyl bromide studied by MALDI-TOF mass spectrometry
    • M. Strohalm, M. Kodicek, and M. Pechar Tryptophan modification by 2-hydroxy-5-nitrobenzyl bromide studied by MALDI-TOF mass spectrometry Biochem. Biophys. Res. Commun. 312 2003 811 816
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 811-816
    • Strohalm, M.1    Kodicek, M.2    Pechar, M.3
  • 15
    • 0022328790 scopus 로고
    • Calculation of molecular volumes and areas for structures of known geometry
    • F.M. Richards Calculation of molecular volumes and areas for structures of known geometry Enzymology 115 1985 440 464
    • (1985) Enzymology , vol.115 , pp. 440-464
    • Richards, F.M.1
  • 16
    • 0029004611 scopus 로고
    • The volume of atoms on the protein surface: Calculated from simulation, using Voronoi polyhedra
    • M. Gerstein, J. Tsai, and M. Levitt The volume of atoms on the protein surface: calculated from simulation, using Voronoi polyhedra J. Mol. Biol. 249 1995 955 966
    • (1995) J. Mol. Biol. , vol.249 , pp. 955-966
    • Gerstein, M.1    Tsai, J.2    Levitt, M.3
  • 20
    • 0035997127 scopus 로고    scopus 로고
    • Effect of stabilizing additives on the structure and hydration of proteins: A study involving monoclinic lysozyme
    • N.T. Saraswathi, R. Sankaranarayanan, and M. Vijayan Effect of stabilizing additives on the structure and hydration of proteins: a study involving monoclinic lysozyme Acta Crystallogr. D Biol. Crystallogr. 58 2002 1162 1167
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 1162-1167
    • Saraswathi, N.T.1    Sankaranarayanan, R.2    Vijayan, M.3
  • 21
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • E. Lindahl, B. Hess, and D. Spoel GROMACS 3.0: a package for molecular simulation and trajectory analysis J. Mol. Mod. 7 2001 306 317
    • (2001) J. Mol. Mod. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Spoel, D.3
  • 22
    • 33645941402 scopus 로고    scopus 로고
    • The OPLS potential functions for proteins: Energy minimization for crystals of cyclic peptides and crambin
    • W.L. Jorgensen, J.T. Rives, The OPLS potential functions for proteins: energy minimization for crystals of cyclic peptides and crambin, J. Am. Chem. Soc. 110 1657-1666
    • J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Rives, J.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.