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Volumn 3, Issue 5, 1999, Pages 564-570

Protein folding and interactions revealed by mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 0032858948     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)00009-5     Document Type: Review
Times cited : (61)

References (46)
  • 1
    • 0029685702 scopus 로고    scopus 로고
    • Analytical properties of the nano-electrospray ion source
    • Wilm M, Mann M Analytical properties of the nano-electrospray ion source. Anal Chem. 68:1996;1-8.
    • (1996) Anal Chem , vol.68 , pp. 1-8
    • Wilm, M.1    Mann, M.2
  • 2
    • 0028064214 scopus 로고
    • Reflecting time of flight mass-spectrometer with an electrospray ion source and orthogonal extraction
    • Verentchikov AN, Ens W, Standing KG Reflecting time of flight mass-spectrometer with an electrospray ion source and orthogonal extraction. Anal Chem. 66:1994;126-133.
    • (1994) Anal Chem , vol.66 , pp. 126-133
    • Verentchikov, A.N.1    Ens, W.2    Standing, K.G.3
  • 3
    • 0031239787 scopus 로고    scopus 로고
    • External accumulation of ions for enhanced electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • Senko MW, Hendrickson CL, Emmett MR, Shi SDH, Marshall AG External accumulation of ions for enhanced electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. J Am Soc Mass Spectrom. 8:1997;970-976.
    • (1997) J Am Soc Mass Spectrom , vol.8 , pp. 970-976
    • Senko, M.W.1    Hendrickson, C.L.2    Emmett, M.R.3    Shi, S.D.H.4    Marshall, A.G.5
  • 4
    • 0029717657 scopus 로고    scopus 로고
    • High sensitivity collisionally-activated decomposition tandem mass spectrometry on a novel quadrupole/orthogonal-acceleration time-of-flight mass spectrometer
    • Morris HR, Paxton T, Dell A, Langhorne J, Berg M, Bordoli RS, Hoyes J, Bateman RH High sensitivity collisionally-activated decomposition tandem mass spectrometry on a novel quadrupole/orthogonal-acceleration time-of-flight mass spectrometer. Rapid Comm Mass Spectrom. 10:1996;889-896.
    • (1996) Rapid Comm Mass Spectrom , vol.10 , pp. 889-896
    • Morris, H.R.1    Paxton, T.2    Dell, A.3    Langhorne, J.4    Berg, M.5    Bordoli, R.S.6    Hoyes, J.7    Bateman, R.H.8
  • 5
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM Electrospray ionization for mass spectrometry of large biomolecules. Science. 246:1989;64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 6
    • 0032550657 scopus 로고    scopus 로고
    • The location of deuterium label in cytochrome c was examined by collision-induced dissociation and, despite extensive scrambling of labile deuterons, the results show that four small helical regions are maintained, even in the most open conformations
    • McLafferty FW, Guan ZQ, Haupts U, Wood TD, Kelleher NL:, Gaseous conformational, structures of, cytochrome c J, Am, Chem, Soc. 120:1998;4732-4740. The location of deuterium label in cytochrome c was examined by collision-induced dissociation and, despite extensive scrambling of labile deuterons, the results show that four small helical regions are maintained, even in the most open conformations.
    • (1998) J, Am, Chem, Soc , vol.120 , pp. 4732-4740
    • McLafferty, F.W.1    Guan, Z.Q.2    Haupts, U.3    Wood, T.D.4    Kelleher, N.5    Gaseous, C.6    Structures, O.7    Cytochrome, C.8
  • 7
    • 0029794153 scopus 로고    scopus 로고
    • Probing the nature of non-covalent interactions by mass spectrometry. A study of protein-CoA ligand binding and assembly
    • Robinson CV, Chung EW, Kragelund BB, Knudsen J, Aplin RT, Poulsen FM, Dobson CM Probing the nature of non-covalent interactions by mass spectrometry. A study of protein-CoA ligand binding and assembly. J Am Chem Soc. 118:1996;8646-8653.
    • (1996) J Am Chem Soc , vol.118 , pp. 8646-8653
    • Robinson, C.V.1    Chung, E.W.2    Kragelund, B.B.3    Knudsen, J.4    Aplin, R.T.5    Poulsen, F.M.6    Dobson, C.M.7
  • 9
    • 0031798478 scopus 로고    scopus 로고
    • Identification of a four copper folding intermediate in mammalian copper metallothionein by electrospray ionization mass spectrometry
    • Jensen LT, Peltier JM, Winge DR Identification of a four copper folding intermediate in mammalian copper metallothionein by electrospray ionization mass spectrometry. J Biol Inorg Chem. 3:1998;627-631.
    • (1998) J Biol Inorg Chem , vol.3 , pp. 627-631
    • Jensen, L.T.1    Peltier, J.M.2    Winge, D.R.3
  • 10
    • 0033556328 scopus 로고    scopus 로고
    • Characterisation of allosteric insulin hexamers by electrospray ionization mass spectrometry
    • Fabris D, Fenselau C Characterisation of allosteric insulin hexamers by electrospray ionization mass spectrometry. Anal Chem. 71:1999;384-387.
    • (1999) Anal Chem , vol.71 , pp. 384-387
    • Fabris, D.1    Fenselau, C.2
  • 11
    • 0032849955 scopus 로고    scopus 로고
    • 2 binding interfaces - evidence from electrospray mass spectrometry
    • in press. This paper shows that under high-energy collision conditions up to three water molecules remain bound to the complex, presumably as a result of hydrogen bonding interactions in the ligand binding interface
    • 2 binding interfaces - evidence from electrospray mass spectrometry. Protein Sci. 1999;. in press. This paper shows that under high-energy collision conditions up to three water molecules remain bound to the complex, presumably as a result of hydrogen bonding interactions in the ligand binding interface.
    • (1999) Protein Sci
    • Chung, E.W.1    Henriques, D.2    Renzoni, D.3    Ladbury, J.E.4    Robinson, C.V.5
  • 12
    • 0033451527 scopus 로고    scopus 로고
    • Binding of aldose reductase inhibitors: Correlation of crystallographic and mass spectrometric studies
    • In this study, both X-ray crystallography and mass spectrometry were applied to aldose reductase and four potential inhibitors and the results were used to demonstrate the complementarity between the two techniques
    • Rogniaux H, Van Dorsselaer A, Barth P, Biellmann JF, Barbanton J, van Zandt M, Chevrier B, Howard E, Mitschler A, Potier Net al. Binding of aldose reductase inhibitors: correlation of crystallographic and mass spectrometric studies. J Am Soc Mass Spectrom. 10:1999;635-647. In this study, both X-ray crystallography and mass spectrometry were applied to aldose reductase and four potential inhibitors and the results were used to demonstrate the complementarity between the two techniques.
    • (1999) J Am Soc Mass Spectrom , vol.10 , pp. 635-647
    • Rogniaux, H.1    Van Dorsselaer, A.2    Barth, P.3    Biellmann, J.F.4    Barbanton, J.5    Van Zandt, M.6    Chevrier, B.7    Howard, E.8    Mitschler, A.9    Potier, N.10
  • 15
    • 0031935288 scopus 로고    scopus 로고
    • Metal mediated sterol receptor-DNA complex association and dissociation by electrospray ionization mass spectrometry
    • Veenstra TD, Benson LM, Craig TA, Tomlinson AJ, Kumar R, Naylor S Metal mediated sterol receptor-DNA complex association and dissociation by electrospray ionization mass spectrometry. Nat Biotechnol. 16:1998;262-266.
    • (1998) Nat Biotechnol , vol.16 , pp. 262-266
    • Veenstra, T.D.1    Benson, L.M.2    Craig, T.A.3    Tomlinson, A.J.4    Kumar, R.5    Naylor, S.6
  • 16
    • 0032528943 scopus 로고    scopus 로고
    • Probing regA/RNA interactions using electrospray ionization Fourier transform ion cyclotron resonance-mass spectrometry
    • Liu CL, Tolic LP, Hofstadler SA, Harms AC, Smith RD, Kang CH, Sinha N Probing regA/RNA interactions using electrospray ionization Fourier transform ion cyclotron resonance-mass spectrometry. Anal Biochem. 262:1998;67-76.
    • (1998) Anal Biochem , vol.262 , pp. 67-76
    • Liu, C.L.1    Tolic, L.P.2    Hofstadler, S.A.3    Harms, A.C.4    Smith, R.D.5    Kang, C.H.6    Sinha, N.7
  • 17
    • 0032463507 scopus 로고    scopus 로고
    • The role of the 6 lysines and the terminal amine of Escherichia coli single-strand binding protein in its binding of single-stranded DNA
    • The authors present a method for covalent modification of lysine residues allowing differential labelling to probe the accessibility of the sidechain amino group and their interactions with DNA
    • Chen JW, Smith DL, Griep MA The role of the 6 lysines and the terminal amine of Escherichia coli single-strand binding protein in its binding of single-stranded DNA. Protein Sci. 7:1998;1781-1788. The authors present a method for covalent modification of lysine residues allowing differential labelling to probe the accessibility of the sidechain amino group and their interactions with DNA.
    • (1998) Protein Sci , vol.7 , pp. 1781-1788
    • Chen, J.W.1    Smith, D.L.2    Griep, M.A.3
  • 18
    • 0032532125 scopus 로고    scopus 로고
    • Direct determination of solution binding constants for noncovalent complexes between bacterial cell wall peptide analogues and vancomycin group antibiotics by electrospray ionization mass spectrometry
    • Jorgensen TJD, Roepstorff P, Heck AJR Direct determination of solution binding constants for noncovalent complexes between bacterial cell wall peptide analogues and vancomycin group antibiotics by electrospray ionization mass spectrometry. Anal Chem. 70:1998;4427-4432.
    • (1998) Anal Chem , vol.70 , pp. 4427-4432
    • Jorgensen, T.J.D.1    Roepstorff, P.2    Heck, A.J.R.3
  • 19
    • 0032533971 scopus 로고    scopus 로고
    • Rapid analysis of epitope-paratope interactions between HIV-1 and a 17-amino-acid neutralizing microantibody by electrospray ionization mass spectrometry
    • A peptide derived from the gp120 envelope glycoprotein of HIV-1 is seen to interact with a specific antibody. Key residues for the interaction are determined, by digestion of the peptide
    • Millar AL, Jackson NAC, Dalton H, Jennings KR, Levi M, Wahren B, Dimmock NJ Rapid analysis of epitope-paratope interactions between HIV-1 and a 17-amino-acid neutralizing microantibody by electrospray ionization mass spectrometry. Eur J Biochem. 258:1998;164-169. A peptide derived from the gp120 envelope glycoprotein of HIV-1 is seen to interact with a specific antibody. Key residues for the interaction are determined, by digestion of the peptide.
    • (1998) Eur J Biochem , vol.258 , pp. 164-169
    • Millar, A.L.1    Jackson, N.A.C.2    Dalton, H.3    Jennings, K.R.4    Levi, M.5    Wahren, B.6    Dimmock, N.J.7
  • 21
  • 22
    • 0032578463 scopus 로고    scopus 로고
    • Counting individual sulfur atoms in a protein by ultra-high resolution Fourier transform ion cyclotron resonance mass spectrometry: Experimental resolution of isotropic fine structure in proteins
    • Shi SDH, Hendrickson CL, Marshall AG Counting individual sulfur atoms in a protein by ultra-high resolution Fourier transform ion cyclotron resonance mass spectrometry: experimental resolution of isotropic fine structure in proteins. Proc Natl Acad Sci USA. 95:1998;11532-11537.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11532-11537
    • Shi, S.D.H.1    Hendrickson, C.L.2    Marshall, A.G.3
  • 24
    • 0032480809 scopus 로고    scopus 로고
    • Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • Changes in the dynamics of the enzyme are revealed by comparing hydrogen exchange mass spectrometry (MS) data of the free and ligand-bound species. Previous crystal structures comparing ligand-free and ligand-bound proteins reveal a flexible loop that closes around an inhibitor. MS reveals that residues screened by closure of this loop have increased protection from HX, and also that regions of the protein that are very similar in the crystal structures have altered HX protection
    • Wang F, Li WQ, Emmett MR, Hendrickson CL, Marshall AG, Zhang YL, Wu L, Zhang ZY Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Biochemistry. 37:1998;15289-15299. Changes in the dynamics of the enzyme are revealed by comparing hydrogen exchange mass spectrometry (MS) data of the free and ligand-bound species. Previous crystal structures comparing ligand-free and ligand-bound proteins reveal a flexible loop that closes around an inhibitor. MS reveals that residues screened by closure of this loop have increased protection from HX, and also that regions of the protein that are very similar in the crystal structures have altered HX protection.
    • (1998) Biochemistry , vol.37 , pp. 15289-15299
    • Wang, F.1    Li, W.Q.2    Emmett, M.R.3    Hendrickson, C.L.4    Marshall, A.G.5    Zhang, Y.L.6    Wu, L.7    Zhang, Z.Y.8
  • 25
    • 0033515632 scopus 로고    scopus 로고
    • Comparison of SH3 and SH2 domain dynamics when expressed alone or in an SH(3+2) construct: The role of protein dynamics in functional regulation
    • Interdomain interactions are shown to alter the dynamics of the individual domains, reflected in alteration of HX characteristics
    • Engen JR, Smithgall TE, Gmeiner WH, Smith DL Comparison of SH3 and SH2 domain dynamics when expressed alone or in an SH(3+2) construct: the role of protein dynamics in functional regulation. J Mol Biol. 287:1999;645-656. Interdomain interactions are shown to alter the dynamics of the individual domains, reflected in alteration of HX characteristics.
    • (1999) J Mol Biol , vol.287 , pp. 645-656
    • Engen, J.R.1    Smithgall, T.E.2    Gmeiner, W.H.3    Smith, D.L.4
  • 26
    • 0033593247 scopus 로고    scopus 로고
    • Defining protein ensembles with native state NH exchange: Kinetics of interconversion and cooperative units from combined NMR and MS analysis
    • NMR-derived HX data of the turkey ovomucoid domain are used to simulate peak widths during mass spectrometry (MS) exchange. Observed MS peaks do not match these, suggesting that the extent of cooperativity is more limited than suggested using NMR
    • Arrington CB, Teesch LM, Robertson AD Defining protein ensembles with native state NH exchange: kinetics of interconversion and cooperative units from combined NMR and MS analysis. J Mol Biol. 285:1999;1265-1275. NMR-derived HX data of the turkey ovomucoid domain are used to simulate peak widths during mass spectrometry (MS) exchange. Observed MS peaks do not match these, suggesting that the extent of cooperativity is more limited than suggested using NMR.
    • (1999) J Mol Biol , vol.285 , pp. 1265-1275
    • Arrington, C.B.1    Teesch, L.M.2    Robertson, A.D.3
  • 27
    • 0000944563 scopus 로고    scopus 로고
    • Electron capture dissociation of multiply charged protein cations. A nonergodic process
    • Zubarev RA, Kelleher Nl, McLafferty FW Electron capture dissociation of multiply charged protein cations. A nonergodic process. J Am Chem Soc. 120:1998;3265-3266.
    • (1998) J Am Chem Soc , vol.120 , pp. 3265-3266
    • Zubarev, R.A.1    Kelleher, N.2    McLafferty, F.W.3
  • 28
    • 0033620364 scopus 로고    scopus 로고
    • Electron capture dissociation of gaseous multiply charged proteins is favoured at disulphide bonds and other sites of high hydrogen atom affinity
    • The electron capture dissociation method was shown to generate preferential cleavage of the backbone at disulfide bonds, in contrast to excitation of the ions by photons or low-energy collisions
    • Zubarev RA, Kruger NA, Frediksson EK, Lewis MA, Horn DM, Carpenter BK, McLafferty FW Electron capture dissociation of gaseous multiply charged proteins is favoured at disulphide bonds and other sites of high hydrogen atom affinity. J Am Chem Soc. 121:1999;2857-2862. The electron capture dissociation method was shown to generate preferential cleavage of the backbone at disulfide bonds, in contrast to excitation of the ions by photons or low-energy collisions.
    • (1999) J Am Chem Soc , vol.121 , pp. 2857-2862
    • Zubarev, R.A.1    Kruger, N.A.2    Frediksson, E.K.3    Lewis, M.A.4    Horn, D.M.5    Carpenter, B.K.6    McLafferty, F.W.7
  • 29
    • 0033541119 scopus 로고    scopus 로고
    • Selective isotope labeling demonstrates that hydrogen exchange at individual peptide amide linkages can be determined by collision-induced dissociation mass spectrometry
    • Hydrogen/deuterium exchange experiments can give site-specific information on the exposure to or protection from solvent of all residues only if the deuterium label remains fixed during digestion, ionisation and fragmentation of proteins. Using cytochrome c as a model, the authors present evidence that the label is not scrambled during peptic digestion or collision-induced dissociation if the b-ions are monitored, as the mass spectrometry results closely match those observed by NMR methods
    • Deng YZ, Pan H, Smith DL Selective isotope labeling demonstrates that hydrogen exchange at individual peptide amide linkages can be determined by collision-induced dissociation mass spectrometry. J Am Chem Soc. 121:1999;1966-1967. Hydrogen/deuterium exchange experiments can give site-specific information on the exposure to or protection from solvent of all residues only if the deuterium label remains fixed during digestion, ionisation and fragmentation of proteins. Using cytochrome c as a model, the authors present evidence that the label is not scrambled during peptic digestion or collision-induced dissociation if the b-ions are monitored, as the mass spectrometry results closely match those observed by NMR methods.
    • (1999) J Am Chem Soc , vol.121 , pp. 1966-1967
    • Deng, Y.Z.1    Pan, H.2    Smith, D.L.3
  • 33
    • 0032765075 scopus 로고    scopus 로고
    • Characterisation of the dominant oxidative folding intermediate of hen lysozyme
    • in press. The refolding of hen egg white lysozyme from a fully unfolded species with reduced cysteine residues is shown to proceed via a stable intermediate with three correctly formed disulfide bonds. The unformed bond is identified by accurate mass measurement by Fourier-transform mass spectrometry (FTMS) followed by digestion of the intermediate and tandem MS of the fragments
    • van den Berg B, Chung EW, Robinson CV, Dobson CM Characterisation of the dominant oxidative folding intermediate of hen lysozyme. J Mol Biol. 1999;. in press. The refolding of hen egg white lysozyme from a fully unfolded species with reduced cysteine residues is shown to proceed via a stable intermediate with three correctly formed disulfide bonds. The unformed bond is identified by accurate mass measurement by Fourier-transform mass spectrometry (FTMS) followed by digestion of the intermediate and tandem MS of the fragments.
    • (1999) J Mol Biol
    • Van Den Berg, B.1    Chung, E.W.2    Robinson, C.V.3    Dobson, C.M.4
  • 34
    • 0032901420 scopus 로고    scopus 로고
    • Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate
    • Tsui V, Garcia C, Cavagnero S, Siuzdak G, Dyson HJ, Wright PE Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate. Protein Sci. 8:1999;45-49.
    • (1999) Protein Sci , vol.8 , pp. 45-49
    • Tsui, V.1    Garcia, C.2    Cavagnero, S.3    Siuzdak, G.4    Dyson, H.J.5    Wright, P.E.6
  • 37
    • 0033580657 scopus 로고    scopus 로고
    • Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behaviour in its disease related variants
    • Human lysozyme variants are shown to refold via short-lived intermediates. One of the variants has markedly different refolding kinetics, observed by the increased lifetime of an intermediate state
    • Canet D, Sunde M, Last AM, Miranker A, Spencer A, Robinson CV, Dobson CM Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behaviour in its disease related variants. Biochemistry. 38:1999;6419-6427. Human lysozyme variants are shown to refold via short-lived intermediates. One of the variants has markedly different refolding kinetics, observed by the increased lifetime of an intermediate state.
    • (1999) Biochemistry , vol.38 , pp. 6419-6427
    • Canet, D.1    Sunde, M.2    Last, A.M.3    Miranker, A.4    Spencer, A.5    Robinson, C.V.6    Dobson, C.M.7
  • 38
    • 0032555738 scopus 로고    scopus 로고
    • Protein subunit interactions and structural integrity of amyloidogenic transthyretins: Evidence from electrospray mass spectrometry
    • The effect of amyloidogenic mutations on the stability of the transthyretin tetramer is shown by comparing the ease of dissociation of the variants with the wild type
    • Nettleton EJ, Sunde M, Lai ZH, Kelly JW, Dobson CM, Robinson CV Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry. J, Mol, Biol. 281:1998;553-564. The effect of amyloidogenic mutations on the stability of the transthyretin tetramer is shown by comparing the ease of dissociation of the variants with the wild type.
    • (1998) J, Mol, Biol , vol.281 , pp. 553-564
    • Nettleton, E.J.1    Sunde, M.2    Lai, Z.H.3    Kelly, J.W.4    Dobson, C.M.5    Robinson, C.V.6
  • 39
    • 0032125821 scopus 로고    scopus 로고
    • Detection of a monomeric intermediate associated with dimerization of protein HU by mass spectrometry
    • The stability of the DNA-binding protein HU is shown to increase with salt concentration. Mass spectrometry also reveals an intermediate, partially folded monomer, which is formed at low salt concentration
    • Vis H, Heinemann U, Dobson CM, Robinson CV Detection of a monomeric intermediate associated with dimerization of protein HU by mass spectrometry. J Am Chem Soc. 120:1998;6427-6428. The stability of the DNA-binding protein HU is shown to increase with salt concentration. Mass spectrometry also reveals an intermediate, partially folded monomer, which is formed at low salt concentration.
    • (1998) J Am Chem Soc , vol.120 , pp. 6427-6428
    • Vis, H.1    Heinemann, U.2    Dobson, C.M.3    Robinson, C.V.4
  • 40
    • 0344655671 scopus 로고    scopus 로고
    • Selective association of protein molecules followed by mass spectrometry
    • Vis H, Dobson CM, Robinson CV Selective association of protein molecules followed by mass spectrometry. Protein Sci. 8:1999;1368-1370.
    • (1999) Protein Sci , vol.8 , pp. 1368-1370
    • Vis, H.1    Dobson, C.M.2    Robinson, C.V.3
  • 41
    • 0032939173 scopus 로고    scopus 로고
    • Crystallographically identical virus capsids display different properties in solution
    • The dynamics of crystallographically identical virus structures are markedly different, despite their identical crystal structures. The recombinant virus, containing a random segment of RNA, is both more rapidly digested and more susceptible to covalent modification than the wild type, which contains the correct viral RNA
    • Bothner B, Schneemann A, Marshall D, Reddy V, Johnson JE, Siuzdak G Crystallographically identical virus capsids display different properties in solution. Nat Struct Biol. 6:1999;114-116. The dynamics of crystallographically identical virus structures are markedly different, despite their identical crystal structures. The recombinant virus, containing a random segment of RNA, is both more rapidly digested and more susceptible to covalent modification than the wild type, which contains the correct viral RNA.
    • (1999) Nat Struct Biol , vol.6 , pp. 114-116
    • Bothner, B.1    Schneemann, A.2    Marshall, D.3    Reddy, V.4    Johnson, J.E.5    Siuzdak, G.6
  • 42
    • 0032499729 scopus 로고    scopus 로고
    • Antiviral agent blocks breathing of the common cold virus
    • X-ray analysis shows that the envelope protein VP4 appears to be buried near the core of human rhinovirus 14, yet is amenable to digestion by trypsin. This shows the large dynamic motions that occur even in this relatively large structure
    • Lewis JK, Bothner B, Smith TJ, Siuzdak G Antiviral agent blocks breathing of the common cold virus. Proc Natl Acad Sci USA. 95:1998;6774-6778. X-ray analysis shows that the envelope protein VP4 appears to be buried near the core of human rhinovirus 14, yet is amenable to digestion by trypsin. This shows the large dynamic motions that occur even in this relatively large structure.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6774-6778
    • Lewis, J.K.1    Bothner, B.2    Smith, T.J.3    Siuzdak, G.4
  • 43
    • 0032247077 scopus 로고    scopus 로고
    • Dissection of multi-protein complexes using mass spectrometry - subunit interactions in transthyretin and retinol-binding protein complexes
    • Rostom AA, Sunde M, Richardson SJ, Schreiber G, Jarvis S, Bateman R, Dobson CM, Robinson CV Dissection of multi-protein complexes using mass spectrometry - subunit interactions in transthyretin and retinol-binding protein complexes. Proteins. 2(suppl):1998;3-11.
    • (1998) Proteins , vol.2 , Issue.SUPPL. , pp. 3-11
    • Rostom, A.A.1    Sunde, M.2    Richardson, S.J.3    Schreiber, G.4    Jarvis, S.5    Bateman, R.6    Dobson, C.M.7    Robinson, C.V.8
  • 44
    • 0032560474 scopus 로고    scopus 로고
    • Mass spectrometry of ribosomes and ribosomal subunits
    • Despite its impressive size, the ribosome can be studied by mass spectrometry. Dissociation products reveal which of the subunits interact strongly, and HX shows how flexible these subunits are within the intact complex
    • Benjamin DR, Robinson CV, Hendrick JP, Hartl FU, Dobson CM Mass spectrometry of ribosomes and ribosomal subunits. Proc Natl Acad Sci USA. 93:1998;7391-7395. Despite its impressive size, the ribosome can be studied by mass spectrometry. Dissociation products reveal which of the subunits interact strongly, and HX shows how flexible these subunits are within the intact complex.
    • (1998) Proc Natl Acad Sci USA , vol.93 , pp. 7391-7395
    • Benjamin, D.R.1    Robinson, C.V.2    Hendrick, J.P.3    Hartl, F.U.4    Dobson, C.M.5
  • 45
    • 0033583731 scopus 로고    scopus 로고
    • Detection of the intact GroEL chaperonin assembly by mass spectrometry
    • The large macromolecular complex of GroEL can be maintained intact in the gas phase. Known connectivities are seen to be preserved upon collision-induced dissociation of the complex, showing that this method could be used to study species where the links are unknown
    • Rostom AA, Robinson CV Detection of the intact GroEL chaperonin assembly by mass spectrometry. J Am Chem Soc. 121:1999;4718-4719. The large macromolecular complex of GroEL can be maintained intact in the gas phase. Known connectivities are seen to be preserved upon collision-induced dissociation of the complex, showing that this method could be used to study species where the links are unknown.
    • (1999) J Am Chem Soc , vol.121 , pp. 4718-4719
    • Rostom, A.A.1    Robinson, C.V.2
  • 46
    • 0032872914 scopus 로고    scopus 로고
    • Disassembly of intact multiprotein complexes in the gas phase
    • Rostom AA, Robinson CV Disassembly of intact multiprotein complexes in the gas phase. Curr Opin Struct Biol. 9:1999;135-141.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 135-141
    • Rostom, A.A.1    Robinson, C.V.2


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